PDB ID CHAIN SEQUENCE POSITION SEQUENCE S1 DISTANCE S1 POSITION S1 ASA  N1 DISTANCE N1 DONOR N1 ID N1 POSITION N1 ASA O1 DISTANCE O1 DONOR O1 ID O1 POSITION O1 ASA ASA EP of S0 pKa of S0 CLASS REF                  STRUCTURE PUBMED ID-1 PUBMED ID-2 MOLECULE OXIDANT LIGAND SOURCE CLASSIFICATION EC #
1A16 A 202 AMAHTRAMEKCRPGMFEYHLE 13.7 249 40.88 6.4 ARG NH1 203 0.34 10 GLU OE2 208 0 0 -16.461 10.86 0 2BWX,1WBQ AMINOPEPTIDASE P SH E-COLI HYDROLASE 3.4.11.9
1A16 A 240 NTIVGSGENGCILHYTENECE 12.9 249 40.88 9.5 ARG NH1 404 0.7 7.4 GLU OE1 237 26.04 0 -21.634 10.28 0 2BWX,1WBQ AMINOPEPTIDASE P SH E-COLI HYDROLASE 3.4.11.9
1A16 A 249 GCILHYTENECEMRDGDLVLI 12.9 240 0 7.4 ARG NH2 252 21.45 4.4 GLU OE1 208 0 41 -17.915 7.41 1 2BWX,1WBQ AMINOPEPTIDASE P SOH E-COLI HYDROLASE 3.4.11.9
1A2L A 30 PQVLEFFSFFCPHCYQFEEVL 3.5 33 0 5.4 HIS NE2 32 29.84 10.1 GLU OE2 24 0.19 6 -14.55 0.53 1 1A2M DsbA UNK SS E-COLI OXIDOREDUCTASE 1
1A2L A 33 LEFFSFFCPHCYQFEEVLHIS 3.5 30 6.39 7.8 HIS NE2 60 0 6.6 GLU OE2 24 0.19 0 -11.738 14.43 1 1A2M DsbA SS E-COLI OXIDOREDUCTASE 1
1ADO A 72 LLTADDRVNPCIGGVILFHET 8.4 338 2.29 8.9 ARG NH1 68 23.11 8.8 ASP OD1 66 1.33 3 -24.777 8.71 1 Sethuraman, M., McComb, M.E., Huang, H., Huang, S., Heibeck, T., Costello, C.E., and Cohen, R.A. 2004. Isotope-coded affinity tag (ICAT) approach to redox proteomics: Identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J. Proteome Res. 3: 1228 -1233. PMID: 15595732. ///// Sygusch, J. and Beaudry, D. 1997. Allosteric communication in mammalian muscle aldolase. Biochem. J. 327: 717-720. PMID: 9581547. 15595732 9581547 D-FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE SS ORYCTOLAGUS CUNICULUS LYASE 4.1.2.13
1ADO A 134 TQGLDGLSERCAQYKKDGADF 4.1 177 0 7.1 ARG NH1 133 0 8.7 GLU OE1 132 5.34 0 -24.515 10.67 0 Sethuraman, M., McComb, M.E., Huang, H., Huang, S., Heibeck, T., Costello, C.E., and Cohen, R.A. 2004. Isotope-coded affinity tag (ICAT) approach to redox proteomics: Identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J. Proteome Res. 3: 1228 -1233. PMID: 15595732. ///// Sygusch, J. and Beaudry, D. 1997. Allosteric communication in mammalian muscle aldolase. Biochem. J. 327: 717-720. PMID: 9581547. 15595732 9581547 D-FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE SH ORYCTOLAGUS CUNICULUS LYASE 4.1.2.13
1ADO A 149 KDGADFAKWRCVLKIGEHTPS 12.2 177 0 9.7 ARG NH1 148 40.01 7.4 GLU OE2 165 11.47 0 -36.232 9.19 0 Sethuraman, M., McComb, M.E., Huang, H., Huang, S., Heibeck, T., Costello, C.E., and Cohen, R.A. 2004. Isotope-coded affinity tag (ICAT) approach to redox proteomics: Identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J. Proteome Res. 3: 1228 -1233. PMID: 15595732. ///// Sygusch, J. and Beaudry, D. 1997. Allosteric communication in mammalian muscle aldolase. Biochem. J. 327: 717-720. PMID: 9581547. 15595732 9581547 D-FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE SH ORYCTOLAGUS CUNICULUS LYASE 4.1.2.13
1ADO A 177 ANVLARYASICQQNGIVPIVE 4.1 134 0 9.1 ARG NH1 133 0 10.3 ASP OD2 109 1.31 0 -31.636 14.18 0 Sethuraman, M., McComb, M.E., Huang, H., Huang, S., Heibeck, T., Costello, C.E., and Cohen, R.A. 2004. Isotope-coded affinity tag (ICAT) approach to redox proteomics: Identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J. Proteome Res. 3: 1228 -1233. PMID: 15595732. ///// Sygusch, J. and Beaudry, D. 1997. Allosteric communication in mammalian muscle aldolase. Biochem. J. 327: 717-720. PMID: 9581547. 15595732 9581547 D-FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE SH ORYCTOLAGUS CUNICULUS LYASE 4.1.2.13
1ADO A 201 LPDGDHDLKRCQYVTEKVLAA 10.6 239 7.65 4.8 HIS NE2 196 0.53 8.5 ASP OD1 197 4.88 6 -24.258 8 1 Sethuraman, M., McComb, M.E., Huang, H., Huang, S., Heibeck, T., Costello, C.E., and Cohen, R.A. 2004. Isotope-coded affinity tag (ICAT) approach to redox proteomics: Identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J. Proteome Res. 3: 1228 -1233. PMID: 15595732. ///// Sygusch, J. and Beaudry, D. 1997. Allosteric communication in mammalian muscle aldolase. Biochem. J. 327: 717-720. PMID: 9581547. 15595732 9581547 D-FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE ? ORYCTOLAGUS CUNICULUS LYASE 4.1.2.13
1ADO A 289 ASINLNAINKCPLLKPWALTF 15.6 201 5.7 5.5 LYS NZ 293 11.41 8.8 GLU OE2 246 41.42 0 -12.867 5.59 0 Sethuraman, M., McComb, M.E., Huang, H., Huang, S., Heibeck, T., Costello, C.E., and Cohen, R.A. 2004. Isotope-coded affinity tag (ICAT) approach to redox proteomics: Identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J. Proteome Res. 3: 1228 -1233. PMID: 15595732. ///// Sygusch, J. and Beaudry, D. 1997. Allosteric communication in mammalian muscle aldolase. Biochem. J. 327: 717-720. PMID: 9581547. 15595732 9581547 D-FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE SH ORYCTOLAGUS CUNICULUS LYASE 4.1.2.13
1ADO A 338 VKRALANSLACQGKYTSSGQA 8.4 72 3.13 9.3 LYS NZ 341 37.03 14.8 GLU OE1 277 5.79 2 -32.045 8.05 1 Sethuraman, M., McComb, M.E., Huang, H., Huang, S., Heibeck, T., Costello, C.E., and Cohen, R.A. 2004. Isotope-coded affinity tag (ICAT) approach to redox proteomics: Identification and quantitation of oxidant-sensitive cysteine thiols in complex protein mixtures. J. Proteome Res. 3: 1228 -1233. PMID: 15595732. ///// Sygusch, J. and Beaudry, D. 1997. Allosteric communication in mammalian muscle aldolase. Biochem. J. 327: 717-720. PMID: 9581547. 15595732 9581547 D-FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE SS ORYCTOLAGUS CUNICULUS LYASE 4.1.2.13
1AO6 A 34 LIAFAQYLQQCPFEDHVKLVN 11.3 91 0 4.5 HIS NE2 39 0.12 4.1 ASP OD2 38 13.42 0.2 -30.814 9.23 1 DeMaster E.G., Quast B.J., Redfern B., Nagasawa H.T. 1995. Reaction of nitric oxide with the free sulfhydryl group of human serum albumin yields a sulfenic acid and nitrous oxide. Biochemistry 34: 11494-11499. PMID: 7547878. 7547878 SERUM ALBUMIN NO SOH HOMO SAPIENS CARRIER PROTEIN                          N/A
1AV8 A 196 LRELKKKLYLCLMSVNALEAI 11.5 272 0.74 7.8 LYS NZ  192 3.77 9 ASP OD1 158 15.5 0 -38.966 11.8 0 1MRR RIBONUCLEOTIDE REDUCTASE R2  SH E-COLI OXIDOREDUCTASE 1.17.4.1
1AV8 A 214 EAIRFYVSFACSFAFAERELM 10.9 305 6.98 10.2 HIS NE2 71 0 8.7 GLU OE1 283 0.37 0 -39.426 12.06 0 1MRR RIBONUCLEOTIDE REDUCTASE R2  SH E-COLI OXIDOREDUCTASE 1.17.4.1
1AV8 A 268 DPEMAEIAEECKQECYDLFVQ 5.7 272 0.74 3.9 LYS NZ  191 4.84 4.3 GLU OE1 271 17.3 4 -21.64 9.59 1 1MRR RIBONUCLEOTIDE REDUCTASE R2  SS E-COLI OXIDOREDUCTASE 1.17.4.1
1AV8 A 272 AEIAEECKQECYDLFVQAAQQ 5.7 268 4.42 7.6 LYS NZ  269 10.45 7 GLU OE1 271 17.3 1 -15.004 11.77 1 1MRR RIBONUCLEOTIDE REDUCTASE R2  SS E-COLI OXIDOREDUCTASE 1.17.4.1
1BQI A 25 PVKNQGSCGCCWAFSAVVTIE 6.2 24 0 5.8 HIS NE2 159 0 7.9 ASP OD1 158 0 15.2 -6.907 1.66 1 Xian, M., Chen, X., Liu, Z., Wang, K., Wang, P.G. 2000. Inhibition of papain by S-nitrosothiols. Formation of mixed disulfides. J Biol Chem. 275: 20467-20473. PMID: 10779505. 10779505 PAPAIN S-Nitrosothiol SNO, intermol SS Carica papaya HYDROLASE 3
1BZH A 92 ILTQGPLPNTCGHFWEMVWEQ 7.4 121 0 7.3 ARG NH2 45 2.42 8.4 ASP OD1 137 6.68 6 -26.444 10.31 0 1OET HUMAN PTP1B  SH HOMO SAPIENS HYDROLASE 3.1.3.48
1BZH A 121 NRVMEKGSLKCAQYWPQKEEK 7.4 92 6.26 4.3 HIS NE2 214 0 8.9 GLU OE2 115 0 0 -21.992 10.47 0 1OET HUMAN PTP1B  SH HOMO SAPIENS HYDROLASE 3.1.3.48
1BZH A 215 SPEHGPVVVHCSAGIGRSGTF 9.2 226 0 5 ARG NH1 221 14.4 7.7 GLU OE1 115 0.85 4 8.135 1.51 1 1OET HUMAN PTP1B  SOH HOMO SAPIENS HYDROLASE 3.1.3.48
1BZH A 231 RSGTFCLADTCLLLMDKRKDP 11 226 0 8.5 ARG NH2 238 22.61 7.7 ASP OD1 245 0.53 0 -13.271 11.68 0 1OET HUMAN PTP1B  SH HOMO SAPIENS HYDROLASE 3.1.3.48
1C25 A 384 NLIKEFVIIDCRYPYEYEGGH 5.9 430 0.71 7.5 HIS NE2 429 0 6.3 ASP OD1 383 0 0 -27.572 11.03 1 Tamura, K., Southwick, E.C., Kerns, J., Rosi, L., Carr, B.I., Wilcox C., and Lazo, J.S. 2000. Cdc25 inhibition and cell cycle arrest by a synthetic thioalkyl vitamin K analogue. Cancer Research 60: 1317–1325. PMID: 10728693 10728693 CDC25A SS HOMO SAPIENS HYDROLASE 3.1.3.48
1C25 A 430 DGKRVIVVFHCEFSSERGPRM 5.9 384 0 6.9 ARG NH1 436 26.55 3.8 GLU OE1 431 1.64 0.7 2.981 6.02 1 Tamura, K., Southwick, E.C., Kerns, J., Rosi, L., Carr, B.I., Wilcox C., and Lazo, J.S. 2000. Cdc25 inhibition and cell cycle arrest by a synthetic thioalkyl vitamin K analogue. Cancer Research 60: 1317–1325. PMID: 10728693 10728693 CDC25A SS HOMO SAPIENS HYDROLASE 3.1.3.48
1C25 A 441 EFSSERGPRMCRYVRERDRLG 9 384 0 6.9 ARG NH2 445 1.47 7.9 ASP OD2 355 18.02 3.1 -19.447 11.26 0 Tamura, K., Southwick, E.C., Kerns, J., Rosi, L., Carr, B.I., Wilcox C., and Lazo, J.S. 2000. Cdc25 inhibition and cell cycle arrest by a synthetic thioalkyl vitamin K analogue. Cancer Research 60: 1317–1325. PMID: 10728693 10728693 CDC25A SH HOMO SAPIENS HYDROLASE 3.1.3.48
1C25 A 476 KGGYKEFFMKCQSYCEPPSYR 7.3 480 0 7.6 LYS NZ  475 27.5 6 GLU OE2 362 8.35 10.1 -17.34 9.14 0 Tamura, K., Southwick, E.C., Kerns, J., Rosi, L., Carr, B.I., Wilcox C., and Lazo, J.S. 2000. Cdc25 inhibition and cell cycle arrest by a synthetic thioalkyl vitamin K analogue. Cancer Research 60: 1317–1325. PMID: 10728693 10728693 CDC25A SH HOMO SAPIENS HYDROLASE 3.1.3.48
1C25 A 480 KEFFMKCQSYCEPPSYRPMHH 7.3 476 10.14 8.1 ARG NH2 385 0 9 ASP OD2 383 0 0 -31.11 8.61 0 Tamura, K., Southwick, E.C., Kerns, J., Rosi, L., Carr, B.I., Wilcox C., and Lazo, J.S. 2000. Cdc25 inhibition and cell cycle arrest by a synthetic thioalkyl vitamin K analogue. Cancer Research 60: 1317–1325. PMID: 10728693 10728693 CDC25A SH HOMO SAPIENS HYDROLASE 3.1.3.48
1CGK A 130 PKSKITHLIVCTTSGVDMPGA 4.2 190 0 10.2 ARG NH2 172 5.81 4.9 GLU OE2 192 0 0 -16.86 11.41 0 1D6I CHALCONE SYNTHASE SH MEDICAGO SATIVA TRANSFERASE 2.3.1.74
1CGK A 164 VKRYMMYQQGCFAGGTVLRLA 7.9 341 0 3.6 HIS NE2 303 0 7.2 GLU OE2 192 0 18 -17.507 4.66 1 1D6I CHALCONE SYNTHASE SOOH MEDICAGO SATIVA TRANSFERASE 2.3.1.74
1CGK A 190 NNKGARVLVVCSEVTAVTFRG 4.2 130 0.02 11.2 HIS NE2 303 0 6.2 GLU OE2 192 0 0 -16.943 13.64 0 1D6I CHALCONE SYNTHASE SH MEDICAGO SATIVA TRANSFERASE 2.3.1.74
1CL0 A 105 RLNGDNGEYTCDALIIATGAS 19.5 303 21.21 7.4 HIS NE2 5 10.24 7.2 ASP OD1 106 18.15 0 -20.793 9.8 0 1TDE THIOREDOXIN REDUCTASE SH E-COLI OXIDOREDUCTASE 1.6.4.5
1CL0 A 135 EAFKGRGVSACATCDGFFYRN 3.1 138 26.32 6.7 HIS NE2 245 8.79 5.2 GLU OE2 160 0.85 14 -23.721 5.34 1 1TDE THIOREDOXIN REDUCTASE SS E-COLI OXIDOREDUCTASE 1.6.4.5
1CL0 A 138 KGRGVSACATCDGFFYRNQKV 3.1 135 13.94 8.9 HIS NE2 245 8.79 5.4 ASP OD2 139 8.37 26 -23.565 16.95 1 1TDE THIOREDOXIN REDUCTASE SS E-COLI OXIDOREDUCTASE 1.6.4.5
1CRU A 338 QDTYNYNDPTCGEMTYICWPT 2.9 345 4.4 7.1 LYS NZ  377 1.02 6.1 ASP OD2 335 22.3 0 -35.43 9.66 1 1C9U SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE SS ACINETOBACTER CALCOACETICUS OXIDOREDUCTASE 1.1.99.17
1CRU A 345 DPTCGEMTYICWPTVAPSSAY 2.9 338 0 6.5 ARG NH1 378 5.96 3.3 ASP OD2 335 22.3 4 -26.982 12.27 1 1C9U SOLUBLE QUINOPROTEIN GLUCOSE DEHYDROGENASE SS ACINETOBACTER CALCOACETICUS OXIDOREDUCTASE 1.1.99.17
1CW3 A 19 PAPNQQPEVFCNQIFINNEWH 10.2 49 0.07 9.8 LYS NZ  209 41.49 9.6 GLU OE2 210 12.27 1 -24.962 10.1 0 1AG8 MITOCHONDRIAL ALDEHYDE DEHYDROGENASE SH HOMO SAPIENS OXIDOREDUCTASE 1.2.1.3
1CW3 A 162 SYTRHEPVGVCGQIIPWNFPL 14.8 128 0 6.7 LYS NZ  240 0.4 7.3 ASP OD2 239 1.2 0 -16.732 11.98 0 1AG8 MITOCHONDRIAL ALDEHYDE DEHYDROGENASE SH HOMO SAPIENS OXIDOREDUCTASE 1.2.1.3
1CW3 A 301 HFALFFNQGQCCCAGSRTFVQ 3.2 303 0 8.9 LYS NZ  112 0.04 4.3 ASP OD1 457 0 1 -23.473 14.39 1 1AG8 MITOCHONDRIAL ALDEHYDE DEHYDROGENASE SS HOMO SAPIENS OXIDOREDUCTASE 1.2.1.3
1CW3 A 303 ALFFNQGQCCCAGSRTFVQED 3.2 301 0.9 11.7 LYS NZ  112 0.04 3.4 ASP OD1 457 0 0 -29.655 19.07 1 1AG8 MITOCHONDRIAL ALDEHYDE DEHYDROGENASE SS HOMO SAPIENS OXIDOREDUCTASE 1.2.1.3
1CW3 A 455 ALQAGTVWVNCYDVFGAQSPF 11.4 303 0 14.8 LYS NZ  127 41.59 9.2 ASP OD1 457 0 20 -20.09 10.37 0 1AG8 MITOCHONDRIAL ALDEHYDE DEHYDROGENASE SH HOMO SAPIENS OXIDOREDUCTASE 1.2.1.3
1D5R A 71 HKNHYKIYNLCAERHYDTAKF 6.1 124 4.28 4.5 ARG NH2 130 0.99 6 GLU OE2 73 1.4 2.5 -8.384 4.15 1 Yu, C.X., Li, S., and Whorton, A.R. 2005. Redox regulation of PTEN by S-nitrosothiols. Mol Pharmacol 68: 847–854. PMID: 15967877. 15967877 PHOSPHOINOSITIDE PHOSPHOTASE PTEN HOOH SS HOMO SAPIENS HYDROLASE 3.1.3.48
1D5R A 83 ERHYDTAKFNCRVAQYPFEDH 15.1 71 2.52 9 ARG NH1 84 19.88 7.6 ASP OD1 58 4.89 0 -27.41 8.84 0 Yu, C.X., Li, S., and Whorton, A.R. 2005. Redox regulation of PTEN by S-nitrosothiols. Mol Pharmacol 68: 847–854. PMID: 15967877. 15967877 PHOSPHOINOSITIDE PHOSPHOTASE PTEN HOOH SH HOMO SAPIENS HYDROLASE 3.1.3.48
1D5R A 124 EDDNHVAAIHCKAGKGRTGVM 6.1 71 2.52 5.2 ARG NH2 130 0.99 7.2 ASP OD2 92 7.59 4.3 13.732 0.72 1 Yu, C.X., Li, S., and Whorton, A.R. 2005. Redox regulation of PTEN by S-nitrosothiols. Mol Pharmacol 68: 847–854. PMID: 15967877. 15967877 PHOSPHOINOSITIDE PHOSPHOTASE PTEN HOOH SS HOMO SAPIENS HYDROLASE 3.1.3.48
1D5R A 136 AGKGRTGVMICAYLLHRGKFL 10.3 105 0 7.9 ARG NH1 172 15.79 8.5 ASP OD2 153 14.56 0 -27.637 10.6 0 Yu, C.X., Li, S., and Whorton, A.R. 2005. Redox regulation of PTEN by S-nitrosothiols. Mol Pharmacol 68: 847–854. PMID: 15967877. 15967877 PHOSPHOINOSITIDE PHOSPHOTASE PTEN HOOH SH HOMO SAPIENS HYDROLASE 3.1.3.48
1DBF A 75 LSGWQYVPVTCMQEMDVTGGL 13.4 88 0 5.8 ARG NH2 63 20.46 12.1 GLU OE2 17 5.96 2 -9.246 10.61 1 1FNJ CHORISMATE MUTASE SOH BACILLUS SUBTILIS ISOMERASE 5.4.99.5
1DBF A 88 EMDVTGGLKKCIRVMMTVQTD 13.4 75 1.6 3.4 ARG NH1 90 0.12 6.5 GLU OE2 78 12.67 0 -10.659 7.49 0 1FNJ CHORISMATE MUTASE SH BACILLUS SUBTILIS ISOMERASE 5.4.99.5
1DE2 A 14 VYGYDSNIHKCVYCDNAKRLL 4.6 17 15.53 7.8 LYS NZ 13 32.53 4.8 ASP OD1 8 0.42 18 -48.226 8.46 1 1DE1 GLUTAREDOXIN SS BACTERIOPHAGE T4 ELECTRON TRANSPORT N/A
1DE2 A 17 YDSNIHKCVYCDNAKRLLTVK 4.6 14 17.93 6.4 LYS NZ 21 48.57 2.9 ASP OD1 8 0.42 16 -23.174 10.19 1 1DE1 GLUTAREDOXIN SS BACTERIOPHAGE T4 ELECTRON TRANSPORT N/A
1DEL A 55 GVFAANTDYPCLTRKEFEGID 19.9 88 0 12.9 LYS NZ 59 46.95 7.2 GLU OE1 60 0 58 -39.884 9 1 1DEK DEOXYNUCLEOSIDE MONOPHOSPHATE KINASE SOOOH BACTERIOPHAGE T4 TRANSFERASE 2.7.4.13
1DLU A 89 EATAWGMNQLCGSGLRAVALG 5.7 378 0.35 4.1 HIS NE2 348 0.95 9 GLU OE1 117 0 9 -6.769 6.26 1 1OU6 BIOSYNTHETIC THIOLASE SOH ZOOGLOEA RAMIGEA TRANSFERASE 2.3.1.9
1EGR A 11 MQTVIFGRSGCPYCVRAKDLA 4.6 14 0 5 ARG NH1 8 7.94 8.3 GLU OE1 57 5.16 20.8 -12.103 9 1 Foloppe, N., Sagemark, J., Nordstrand, K., Berndt, K.D., and Nilsson, L. 2001. Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: Comparison with functionally related proteins. J. Mol. Biol. 310: 449-470. PMID: 11428900. 11428900 GLUTAREDOXIN SS ESCHERICHIA COLI                                 ELECTRON TRANSPORT                       N/A
1EGR A 14 VIFGRSGCPYCVRAKDLAEKL 4.6 11 20.75 6.9 ARG NH1 8 7.94 8 ASP OD1 37 0 0 -11.948 7.4 1 Foloppe, N., Sagemark, J., Nordstrand, K., Berndt, K.D., and Nilsson, L. 2001. Structure, dynamics and electrostatics of the active site of glutaredoxin 3 from Escherichia coli: Comparison with functionally related proteins. J. Mol. Biol. 310: 449-470. PMID: 11428900. 11428900 GLUTAREDOXIN SS ESCHERICHIA COLI                                 ELECTRON TRANSPORT                       N/A
1ERT A 32 LVVVDFSATWCGPCKMIKPFF 3.9 35 0 8.3 LYS NZ 36 37.86 9.2 ASP OD1 26 0.09 13 -19.052 6.44 1 1ERU HUMAN THIOREDOXIN SS HOMO SAPIENS OXIDOREDUCTASE 1
1ERT A 35 VDFSATWCGPCKMIKPFFHSL 3.9 32 13.4 9 LYS NZ 36 37.86 5.5 ASP OD1 26 0.09 0 -31.626 8.56 1 1ERU HUMAN THIOREDOXIN SS HOMO SAPIENS OXIDOREDUCTASE 1
1ERT A 69 VDDCQDVASECEVKCMPTFQF 9.8 62 1.67 6.8 LYS NZ 85 23.61 6.9 GLU OE1 68 12.6 15 -33.674 9.52 0 1ERU HUMAN THIOREDOXIN SH HOMO SAPIENS OXIDOREDUCTASE 1
1ERT A 73 QDVASECEVKCMPTFQFFKKG 9.1 32 13.4 7.6 LYS NZ 72 24.77 8.5 GLU OE2 88 12.95 56 -17.661 9 0 1ERU HUMAN THIOREDOXIN SH HOMO SAPIENS OXIDOREDUCTASE 1
1ESQ A 9 --MDAQSAAKCLTAVRRHSPL 9.9 208 0 10 LYS NZ 8 30.56 4.1 GLU OE2 211 22.79 12 -21.163 9.6 0 1EKK HYDROXYETHYLTHIAZOLE KINASE SH BACILLUS SUBTILIS TRANSFERASE 2.7.1.50
1ESQ A 198 KLLTKVTGAGCLLTSVVGAFC 16.2 208 0 5.9 ARG NH2 121 7.9 4.5 ASP OD2 94 0.01 9 -25.237 10.36 1 1EKK HYDROXYETHYLTHIAZOLE KINASE SOOH BACILLUS SUBTILIS TRANSFERASE 2.7.1.50
1ESQ A 208 CLLTSVVGAFCAVEENPLFAA 9.9 9 12.13 13.5 ARG NH2 121 7.9 9 GLU OE1 211 11.37 0 -31.012 11.5 0 1EKK HYDROXYETHYLTHIAZOLE KINASE SH BACILLUS SUBTILIS TRANSFERASE 2.7.1.50
1F5A A 36 ISLAAPKETDCLLTQKLVETL 16.6 257 0.91 12 LYS NZ 41 24.92 7.5 GLU OE1 33 39.11 60 -23.562 9 1 1Q79 POLY(A) POLYMERASE SOOH BOS TAURUS TRANSFERASE 2.7.7.19
1F5A A 118 HTKGADIDALCVAPRHVDRSD 10.8 204 1.42 9.5 ARG NH1 126 0.41 10.8 ASP OD2 128 0.68 0 -21.254 11.86 0 1Q79 POLY(A) POLYMERASE SH BOS TAURUS TRANSFERASE 2.7.7.19
1F5A A 160 EEAFVPVIKLCFDGIEIDILF 19.1 118 0 6.3 ARG NH2 147 0.9 4.9 GLU OE1 165 26.43 30 -18.479 8.16 0 1Q79 POLY(A) POLYMERASE SH BOS TAURUS TRANSFERASE 2.7.7.19
1F5A A 197 DSLLKNLDIRCIRSLNGCRVT 11 118 0 4.3 ARG NH2 126 0 5.3 ASP OD1 194 0 5 -0.41 2.99 1 1Q79 POLY(A) POLYMERASE SOOH BOS TAURUS TRANSFERASE 2.7.7.19
1F5A A 293 NPVLLKQPEECNLNLPVWDPR 16.9 197 4.72 3.9 LYS NZ 191 8.6 4.8 ASP OD2 187 25.05 18 -20.584 8.87 0 1Q79 POLY(A) POLYMERASE SH BOS TAURUS TRANSFERASE 2.7.7.19
1FPZ A 70 VQKDTEELKSCGIQDIFVFCT 10.4 46 2.84 5.5 LYS NZ  135 27.9 4.4 GLU OE1 66 25.99 34.2 -24.515 9.07 0 Johnson, L.N., De Moliner, E., Brown, N.R., Song, H., Barford, D., Endicott, J.A., and Noble, M.E. 2002. Structural studies with inhibitors of the cell cycle regulatory kinase cyclin-dependent protein kinase 2. Pharmacol Ther. 93:113-124. PMID: 12191604. 12191604 CYCLIN-DEPENDENT KINASE INHIBITOR 11 SH HOMO SAPIENS HYDROLASE 3.1.3.48
1FPZ A 79 SCGIQDIFVFCTRGELSKYRV 5.4 140 0.01 4.5 ARG NH2 146 2.14 3.8 GLU OE1 83 0.04 0 -17.393 9.43 1 Johnson, L.N., De Moliner, E., Brown, N.R., Song, H., Barford, D., Endicott, J.A., and Noble, M.E. 2002. Structural studies with inhibitors of the cell cycle regulatory kinase cyclin-dependent protein kinase 2. Pharmacol Ther. 93:113-124. PMID: 12191604. 12191604 CYCLIN-DEPENDENT KINASE INHIBITOR 5 SS HOMO SAPIENS HYDROLASE 3.1.3.48
1FPZ A 119 ADGGTPDIASCCEIMEELTTC 4.2 153 0.4 8.1 LYS NZ  195 16.35 7.9 ASP OD1 115 0.23 0.4 -28.272 9.94 0 Johnson, L.N., De Moliner, E., Brown, N.R., Song, H., Barford, D., Endicott, J.A., and Noble, M.E. 2002. Structural studies with inhibitors of the cell cycle regulatory kinase cyclin-dependent protein kinase 2. Pharmacol Ther. 93:113-124. PMID: 12191604. 12191604 CYCLIN-DEPENDENT KINASE INHIBITOR 3 SH HOMO SAPIENS HYDROLASE 3.1.3.48
1FPZ A 140 LKNYRKTLIHCYGGLGRSCLV 5.4 79 0 4.5 ARG NH2 146 2.14 6.8 GLU OE2 83 0.35 0 -19.058 4.12 1 Johnson, L.N., De Moliner, E., Brown, N.R., Song, H., Barford, D., Endicott, J.A., and Noble, M.E. 2002. Structural studies with inhibitors of the cell cycle regulatory kinase cyclin-dependent protein kinase 2. Pharmacol Ther. 93:113-124. PMID: 12191604. 12191604 CYCLIN-DEPENDENT KINASE INHIBITOR 6 SS HOMO SAPIENS HYDROLASE 3.1.3.48
1FPZ A 148 IHCYGGLGRSCLVAACLLLYL 8.2 140 0.01 6.6 ARG NH2 175 29.96 11.1 ASP OD2 173 20.11 0 -15.227 7.83 0 Johnson, L.N., De Moliner, E., Brown, N.R., Song, H., Barford, D., Endicott, J.A., and Noble, M.E. 2002. Structural studies with inhibitors of the cell cycle regulatory kinase cyclin-dependent protein kinase 2. Pharmacol Ther. 93:113-124. PMID: 12191604. 12191604 CYCLIN-DEPENDENT KINASE INHIBITOR 9 SH HOMO SAPIENS HYDROLASE 3.1.3.48
1FPZ A 153 GLGRSCLVAACLLLYLSDTIS 4.2 119 0.39 8.7 LYS NZ  195 16.35 10.5 GLU OE1 191 19.45 0.4 -20.211 13.48 0 Johnson, L.N., De Moliner, E., Brown, N.R., Song, H., Barford, D., Endicott, J.A., and Noble, M.E. 2002. Structural studies with inhibitors of the cell cycle regulatory kinase cyclin-dependent protein kinase 2. Pharmacol Ther. 93:113-124. PMID: 12191604. 12191604 CYCLIN-DEPENDENT KINASE INHIBITOR 4 SH HOMO SAPIENS HYDROLASE 3.1.3.48
1FTN A 16 KKLVIVGDGACGKTCLLIVNS 5.1 83 0 4.1 LYS NZ  18 5.3 6.8 ASP OD1 13 2.4 0 -10.725 7.73 1 Heo, J., Raines, K.W., Mocanu, V., and Campbell, S.L. 2006. Redox regulation of RhoA. Biochem. 45: 14481-14489. PMID: 17128987. 17128987 RhoA SS HOMO SAPIENS PROTO ONCOGENE N/A
1FTN A 20 IVGDGACGKTCLLIVNSKDQF 10.3 16 0 7.9 LYS NZ  118 32.06 8.6 GLU OE1 32 14.84 17 -13.67 9.34 1 Heo, J., Raines, K.W., Mocanu, V., and Campbell, S.L. 2006. Redox regulation of RhoA. Biochem. 45: 14481-14489. PMID: 17128987. 17128987 RhoA SS HOMO SAPIENS PROTO ONCOGENE N/A
1FTN A 83 SYPDTDVILMCFSIDSPDSLE 5.1 16 0 7.1 LYS NZ  18 5.3 8.4 ASP OD1 59 0 0 -25.413 13.17 0 Heo, J., Raines, K.W., Mocanu, V., and Campbell, S.L. 2006. Redox regulation of RhoA. Biochem. 45: 14481-14489. PMID: 17128987. 17128987 RhoA SH HOMO SAPIENS PROTO ONCOGENE N/A
1FTN A 107 EKWTPEVKHFCPNVPIILVGN 14.3 83 0 7.8 LYS NZ  7 3.08 8.4 GLU OE2 102 0 2 -21.887 9.33 0 Heo, J., Raines, K.W., Mocanu, V., and Campbell, S.L. 2006. Redox regulation of RhoA. Biochem. 45: 14481-14489. PMID: 17128987. 17128987 RhoA SH HOMO SAPIENS PROTO ONCOGENE N/A
1FTN A 159 NRIGAFGYMECSAKTKDGVRE 7 83 0 7.2 LYS NZ  119 2.18 8.2 ASP OD1 120 2.28 0 -19.335 10.9 0 Heo, J., Raines, K.W., Mocanu, V., and Campbell, S.L. 2006. Redox regulation of RhoA. Biochem. 45: 14481-14489. PMID: 17128987. 17128987 RhoA SH HOMO SAPIENS PROTO ONCOGENE N/A
1GU9 A 130 WSFAVSAINGCSHCLVAHEHT 3.5 133 3.82 6.7 ARG NH1 86 20.94 11.6 ASP OD1 96 1.99 0 -2.144 2.2 1 Koshkin, A., Nunn, C.M., Djordjevic, S., and Ortiz de Montellano, P.R. 2003. The mechanism of mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics. J. Biol. Chem. 278: 29502-29508. PMID: 12761216. 12761216 ALKYLHYDROPEROXIDASE D SS MYCOBACTERIUM TUBERCULOSIS OXIDOREDUCTASE 1
1GU9 A 133 AVSAINGCSHCLVAHEHTLRT 3.5 130 0.04 5.2 HIS NE2 137 13.26 9.7 GLU OE2 118 0.55 3.8 -14.167 11.09 1 Koshkin, A., Nunn, C.M., Djordjevic, S., and Ortiz de Montellano, P.R. 2003. The mechanism of mycobacterium tuberculosis alkylhydroperoxidase AhpD as defined by mutagenesis, crystallography, and kinetics. J. Biol. Chem. 278: 29502-29508. PMID: 12761216. 12761216 ALKYLHYDROPEROXIDASE D SS MYCOBACTERIUM TUBERCULOSIS OXIDOREDUCTASE 1
1GXF A 53 PPFFSALGGTCVNVGCVPKKL 4.1 58 28.26 9.6 LYS NZ 61 14.57 10.4 ASP OD2 327 15.68 20 -0.434 6.46 1 1AOG TRYPANOTHIONE REDUCTASE SS TRYPANOSOMA CRUZI OXIDOREDUCTASE 1.6.4.8
1GXF A 58 ALGGTCVNVGCVPKKLMVTGA 4.1 53 20.02 5.8 LYS NZ 61 14.57 8.4 GLU OE1 203 2.59 28 -0.359 1.87 1 1AOG TRYPANOTHIONE REDUCTASE SS TRYPANOSOMA CRUZI OXIDOREDUCTASE 1.6.4.8
1GXF A 176 HMPNIPGIEHCISSNEAFYLP 10.1 221 0.37 7.9 HIS NE2 175 12.32 8 GLU OE1 174 14.79 0 -0.048 9.73 0 1AOG TRYPANOTHIONE REDUCTASE SH TRYPANOSOMA CRUZI OXIDOREDUCTASE 1.6.4.8
1GXF A 375 AVFSIPPIGTCGLIEEVASKR 9.4 444 43.76 8.5 HIS NE2 428 0 10.2 ASP OD2 358 10.83 0 -0.055 11.42 0 1AOG TRYPANOTHIONE REDUCTASE SH TRYPANOSOMA CRUZI OXIDOREDUCTASE 1.6.4.8
1GXF A 469 GVHPTSAEELCSMRTPSYYYV 8.5 444 43.76 7.6 ARG NH2 472 22.14 7.8 GLU OE1 466 10.05 22 -0.067 10.71 0 1AOG TRYPANOTHIONE REDUCTASE SH TRYPANOSOMA CRUZI OXIDOREDUCTASE 1.6.4.8
1HL3 A 27 PLVALLDGRDCTVEMPILKDV 9.4 43 1.45 6.6 ARG NH2 317 0 4.9 GLU OE1 30 0 2 -28.519 10.89 1 1HKU C-TERMINAL BINDING PROTEIN 3 SOH RATTUS NORVEGICUS TRANSCRIPTION CO REPRESOR N/A
1HL3 A 226 LFHSDCVTLHCGLNEHNHHLI 14.3 221 0.11 9.2 HIS NE2 225 0 7.9 ASP OD2 193 10.96 1 -28.722 9.51 0 1HKU C-TERMINAL BINDING PROTEIN 3 SH RATTUS NORVEGICUS TRANSCRIPTION CO REPRESOR N/A
1HN9 A 103 QIQSMLGIKGCPAFDVAAACA 8.9 92 37.83 11 LYS NZ 70 18.98 10.5 ASP OD2 71 6.14 1 -41.465 10.66 0 1MZS BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III SH E-COLI TRANSFERASE 2.3.1.41
1HN9 A 112 GCPAFDVAAACAGFTYALSVA 10.1 146 0.12 4 HIS NE2 244 0 6.6 ASP OD2 140 0.06 9 -29.812 6.96 1 1MZS BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III SOOOH E-COLI TRANSFERASE 2.3.1.41
1HN9 A 146 VVGSDVLARTCDPTDRGTIII 10.1 112 8.9 6.9 ARG NH2 17 0.77 6.7 ASP OD2 150 5.73 0 -21.117 10.36 0 1MZS BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III SH E-COLI TRANSFERASE 2.3.1.41
1HN9 A 282 HGNTSAASVPCALDEAVRDGR 12.8 112 8.9 6.1 HIS NE2 272 6.93 6.8 ASP OD1 285 5.61 0 -24.886 10.94 0 1MZS BETA-KETOACYL-ACYL CARRIER PROTEIN SYNTHASE III SH E-COLI TRANSFERASE 2.3.1.41
1HW7 A 141 VGLEGDTLAACLEDYFMRSEQ 38.4 232 29.92 6.6 LYS NZ 107 18.71 5.2 ASP OD2 144 9.31 0 -14.352 7.16 0 Barbirz, S., Jakob, U., and Glocker, M.O. 2000. Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone. J Biol Chem. 275: 18759-18766. PMID: 10764757. 10764757 HSP3 HEAT SHOCK HOOH SH E-COLI CHAPERONE N/A
1HW7 A 232 VYDPQDVEFKCTC-------- 3.5 234 57.32 10.7 LYS NZ 231 45.9 10.4 GLU OE2 229 30.28 30 -16.415 6.31 1 Barbirz, S., Jakob, U., and Glocker, M.O. 2000. Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone. J Biol Chem. 275: 18759-18766. PMID: 10764757. 10764757 HSP3 HEAT SHOCK HOOH SS E-COLI CHAPERONE N/A
1HW7 A 234 DPQDVEFKCTC---------- 3.5 232 29.92 13.4 LYS NZ 231 45.9 13.8 GLU OE2 229 30.28 57 -14.384 7.86 1 Barbirz, S., Jakob, U., and Glocker, M.O. 2000. Mass spectrometry unravels disulfide bond formation as the mechanism that activates a molecular chaperone. J Biol Chem. 275: 18759-18766. PMID: 10764757. 10764757 HSP3 HEAT SHOCK HOOH SS E-COLI CHAPERONE N/A
1I69 A 199 EKLLMLEDGHCLRDQAMGFCF 19 208 67.52 5.4 ARG NH1 266 0 7.2 ASP OD2 202 7.99 2 -12.575 7.18 1 1I6A OXYR HOOH SS E-COLI TRANSCRIPTION  N/A
1I69 A 208 HCLRDQAMGFCFDTHFRATSL 19 199 1.54 11.8 LYS NZ 190 25.05 13.9 ASP OD1 202 20.13 68 -21.469 8.3 1 1I6A OXYR HOOH SS E-COLI TRANSCRIPTION  N/A
1I9S A 97 IKLQCKGHGECPTTENTETFI 9.8 91 0 3.9 ARG NH2 176 11.35 5.1 GLU OE2 172 2.91 15 -20.645 6.99 0 1I9T RNA TRIPHOSPHATASE  SH MUS MUSCULUS HYDROLASE 3.1.3.33
1I9S A 110 TENTETFIRLCERFPELIGVH 11.3 91 0 6.7 ARG NH2 23 7.37 9.3 GLU OE1 111 12.52 0 -17.007 10.44 0 1I9T RNA TRIPHOSPHATASE  SH MUS MUSCULUS HYDROLASE 3.1.3.33
1I9S A 126 ERFPELIGVHCTHGFNRTGFL 8.5 91 0 6.9 ARG NH1 132 12.29 8.4 ASP OD1 66 0 7 10.951 1.62 1 1I9T RNA TRIPHOSPHATASE  SOH MUS MUSCULUS HYDROLASE 3.1.3.33
1I9S A 138 HGFNRTGFLICAFLVEKMDWS 12.2 97 15.05 11.5 ARG NH1 176 0.12 10.6 GLU OE1 150 7.51 0 -15.134 11.26 0 1I9T RNA TRIPHOSPHATASE  SH MUS MUSCULUS HYDROLASE 3.1.3.33
1I9S A 193 APPPPVLPDWCFEDED----- 8 13 0.74 5.8 ARG NH1 9 8.07 8.3 ASP OD1 191 32.09 7 -9.122 8.64 0 1I9T RNA TRIPHOSPHATASE  SH MUS MUSCULUS HYDROLASE 3.1.3.33
1JC0 A 70 WPTLVTTLVQCFSRYPDHMKR 17.6 204 41 6.9 LYS NZ 85 0.1 7.8 ASP OD1 82 0 0 -12.514 10.88 0 1JC1 GREEN FLUORESCENT PROTEIN SH AEQUOREA VICTORIA LUMINSCENT PROTEIN N/A
1JC0 A 147 LGHKLEYNYNCHNVYIMADKQ 3.4 204 41 7.6 HIS NE2 148 0 9.6 GLU OE1 222 9.26 35 -15.51 9.14 1 1JC1 GREEN FLUORESCENT PROTEIN SS AEQUOREA VICTORIA LUMINSCENT PROTEIN N/A
1JC0 A 204 LLPDNHYLSTCSALSKDPNEK 3.4 147 35.28 9.9 HIS NE2 148 0 8.7 GLU OE2 222 9.48 41 -29.142 9.07 1 1JC1 GREEN FLUORESCENT PROTEIN SS AEQUOREA VICTORIA LUMINSCENT PROTEIN N/A
1JQD A 31 RFLNHSTEHQCMQEFMDKKLP 12.3 217 10.94 10.1 LYS NZ 39 42.55 5.9 GLU OE1 34 33.22 1 -21.562 9.66 0 2AOT HISTAMINE METHYLTRANSFERASE SH HOMO SAPIENS TRANSFERASE 2.1.1.8
1JQD A 82 SKVQAQYPGVCINNEVVEPSA 32.1 31 1.01 6.5 LYS NZ 112 47.45 6.4 GLU OE2 53 20.33 62 -19.246 8.74 1 2AOT HISTAMINE METHYLTRANSFERASE SOH HOMO SAPIENS TRANSFERASE 2.1.1.8
1JQD A 217 MLDNLGLKYECYDLLSTMDIS 12.3 31 1.01 12.2 LYS NZ 39 42.55 4.2 ASP OD2 219 1.83 11 -16.662 10.94 1 2AOT HISTAMINE METHYLTRANSFERASE SOH HOMO SAPIENS TRANSFERASE 2.1.1.8
1JQD A 229 DLLSTMDISDCFIDGNENGDL 15.5 248 13.91 7.5 ARG NH2 259 26.04 7.1 ASP OD1 238 3.26 0 -26.513 10.62 0 2AOT HISTAMINE METHYLTRANSFERASE SH HOMO SAPIENS TRANSFERASE 2.1.1.8
1JQD A 248 DLLWDFLTETCNFNATAPPDL 13.5 196 27.91 4.9 LYS NZ 14 14.78 6 ASP OD1 242 5.36 14 -26.136 9.07 1 2AOT HISTAMINE METHYLTRANSFERASE SOH HOMO SAPIENS TRANSFERASE 2.1.1.8
1K3I A 18 AISRNNWAVTCDSAQSGNECN 3.8 27 0 10.1 HIS NE2 53 0 5.5 ASP OD1 19 0 8 -20.432 8.17 1 1GOF GALACTOSE OXIDASE PRECURSOR   SS FUSARIUM SPP OXIDOREDUCTASE 1.1.3.9
1K3I A 27 TCDSAQSGNECNKAIDGNKDT 3.8 18 7.91 11.1 ARG NH1 11 0 8.2 ASP OD1 19 0 0 -29.415 11.91 1 1GOF GALACTOSE OXIDASE PRECURSOR   SS FUSARIUM SPP OXIDOREDUCTASE 1.1.3.9
1LJL A 10 --DKKTIYFICTGNSCRSQMA 5.7 82 1.69 5.6 ARG NH2 16 14.25 7.8 ASP OD1 105 3.51 3 1.022 -0.42 1 1LK0 ARSENATE REDUCTASE SS STAPHYLOCOCCUS AUREUS OXIDOREDUCTASE 1.97.1.5
1LJL A 15 TIYFICTGNSCRSQMAEGWGK 6.8 10 3.34 7.2 ARG NH2 16 14.25 5.4 ASP OD1 105 3.51 2 -14.005 9.29 0 1LK0 ARSENATE REDUCTASE SH STAPHYLOCOCCUS AUREUS OXIDOREDUCTASE 1.97.1.5
1LJL A 82 LKQSDLVVTLCSDADNNCPIL 5.7 10 3.34 4.1 ARG NH2 16 14.25 5.5 ASP OD2 84 37.29 2 -17.524 1.76 1 1LK0 ARSENATE REDUCTASE SS STAPHYLOCOCCUS AUREUS OXIDOREDUCTASE 1.97.1.5
1LOR A 65 IIAEFRKRFGCRIIADFKVAD 22.2 84 0 3.9 ARG NH2 35 32.2 6.8 ASP OD1 39 11.93 0 -16.373 8.11 1 1LOQ OROTIDINE MONOPHOSPHATE DECARBOXYLASE SOH METHANOBACTERIUM THERMOAUTOTROPHICUM LYASE 4.1.1.23
1LOR A 109 GFPGADSVRACLNVAEEMGRE 3.4 84 0 10.5 ARG NH1 107 26.17 9.7 GLU OE2 81 10.47 0 -16.002 9.67 0 1LOQ OROTIDINE MONOPHOSPHATE DECARBOXYLASE SH METHANOBACTERIUM THERMOAUTOTROPHICUM LYASE 4.1.1.23
1MMT A 217 NHIFPLLEKYCGFHEDNIPQL 7.6 237 19.54 9.2 HIS NE2 220 17.53 7.4 ASP OD2 229 18.28 1 -29.269 10.22 1 1TDW PHENYLALANINE-4-HYDROXYLASE  SS HOMO SAPIENS OXIDOREDUCTASE 1.14.16.1
1MMT A 334 IYWFTVEFGLCKQGDSIKAYG 5.3 203 0.08 9.3 LYS NZ  341 21.99 5.6 GLU OE1 205 1.18 1 -30.397 11.87 1 1TDW PHENYLALANINE-4-HYDROXYLASE  SS HOMO SAPIENS OXIDOREDUCTASE 1.14.16.1
1MMT A 357 LLSSFGELQYCLSEKPKLLPL 10.4 334 1.4 6.5 HIS NE2 201 11.75 7 GLU OE1 353 0 0 -24.489 10.84 0 1TDW PHENYLALANINE-4-HYDROXYLASE  SH HOMO SAPIENS OXIDOREDUCTASE 1.14.16.1
1MR8 A 42 DDLKKLLETECPQYIRKKGAD ? ? ? 9.3 ARG NH1 47 36.47 7.5 GLU OE1 41 23.83 3.3 -39.317 10.42 1 Vogl, T., Roth, J., Sorg, C., Hillenkamp, F., and Strupat, K. 1999. Calcium-induced noncovalently linked tetramers of MRP8 and MRP14 detected by ultraviolet matrix-assisted laser desorption/ionization mass spectrometry. J Am Soc Mass Spectrom. 10: 1124-1130. PMID: 10536818. 10536818 MIGRATION INHIBITORY FACTOR-RELATED PROTEIN 8 intermol SS HOMO SAPIENS METAL TRANSPORT                          N/A
1N2F A 60 EQLFAAGYSACFIGAMKFVAG 3.6 124 0 10.6 ARG NH2 131 0.02 17.1 ASP OD2 26 33.29 16.3 -9.639 10.63 1 Lesniak, J., Barton, W.A., and Nikolov, D.B. 2002. Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr. EMBO J 21: 6649-6659. PMID: 12485986.  12485986 ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN HOOH SS PSEUDOMONAS AERUGINOSA PAO1 OXIDOREDUCTASE 1
1N2F A 124 EALVAAAHQVCPYSNATRGNI 3.6 60 16.26 7.2 HIS NE2 121 1.32 14.8 ASP OD1 135 22.2 0 -9.685 6.94 1 Lesniak, J., Barton, W.A., and Nikolov, D.B. 2002. Structural and functional characterization of the Pseudomonas hydroperoxide resistance protein Ohr. EMBO J 21: 6649-6659. PMID: 12485986.  12485986 ORGANIC HYDROPEROXIDE RESISTANCE PROTEIN HOOH SS PSEUDOMONAS AERUGINOSA PAO1 OXIDOREDUCTASE 1
1NHQ A 42 EKGDFISFLSCGMQLYLEGKV ? ? ? 4.2 HIS NE2 10 3 7.6 GLU OE1 163 9.42 33 -19.822 6.18 1 1JOA NADH PEROXIDASE  SOH ENTEROCOCCUS FAECALIS OXIDOREDUCTASE 1.11.1.1
1NTM H 30 VREQCEQLEKCVKARERLELC 5.3 24 0 7.5 ARG NH1 65 0.79 8 GLU OE1 25 13.75 3 -24.508 8.53 0 1BCC UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I, MITOCHONDRIAL SH BOS TAURUS OXIDOREDUCTASE 1.10.2.2
1NTM H 40 CVKARERLELCDERVSSRSQT 3.7 54 3.21 3.4 ARG NH2 43 25.74 3.2 GLU OE2 57 16.83 1 -28.426 8.76 1 1BCC UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I, MITOCHONDRIAL SS BOS TAURUS OXIDOREDUCTASE 1.10.2.2
1NTM H 54 VSSRSQTEEDCTEELLDFLHA 3.7 40 0.46 6.9 ARG NH2 43 25.74 3.9 ASP OD1 41 24.93 3 -38.792 10.46 1 1BCC UBIQUINOL-CYTOCHROME C REDUCTASE COMPLEX CORE PROTEIN I, MITOCHONDRIAL SS BOS TAURUS OXIDOREDUCTASE 1.10.2.2
1O4B A 44 RESETTKGAYCLSVSDFDNAK 11.5 97 0 3.3 ARG NH1 34 4.29 8.3 GLU OE1 37 28.5 9 -13.299 0.67 1 1O4C PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC SOH HOMO SAPIENS TRANSFERASE 2.7.1.112
1OKG A 33 DHLAEYRIVDCRYSLKIKDHG 4.9 100 0 8.5 ARG NH1 57 1.17 6.5 ASP OD1 32 0.36 0 -23.934 11 0 Nagahara, N. and Katayama, A. 2005. Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteinesulfenate in the maintenance of redox homeostasis. J Biol Chem. 280: 34569-34576. PMID: 16107337. 16107337 POSSIBLE 3-MERCAPTOPYRUVATE SULFURTRANSFERASE HOOH or tetrathionate SH LEISHMANIA MAJOR TRANSFERASE 2.8.1.2
1OKG A 134 AYVINGGFQACKAAGLEESGE 10.6 105 0 8.8 ARG NH2 34 0 8.8 ASP OD2 32 0 2.4 -26.975 10.68 0 Nagahara, N. and Katayama, A. 2005. Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteinesulfenate in the maintenance of redox homeostasis. J Biol Chem. 280: 34569-34576. PMID: 16107337. 16107337 POSSIBLE 3-MERCAPTOPYRUVATE SULFURTRANSFERASE HOOH or tetrathionate SH LEISHMANIA MAJOR TRANSFERASE 2.8.1.2
1OKG A 247 HNITVVQADLCSFVFSGSGVT 14.9 260 0 5.3 HIS NE2 164 0 2.9 ASP OD2 245 0.3 17.1 -13.003 7.68 1 Nagahara, N. and Katayama, A. 2005. Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteinesulfenate in the maintenance of redox homeostasis. J Biol Chem. 280: 34569-34576. PMID: 16107337. 16107337 POSSIBLE 3-MERCAPTOPYRUVATE SULFURTRANSFERASE HOOH or tetrathionate SOH LEISHMANIA MAJOR TRANSFERASE 2.8.1.2
1OKG A 260 FVFSGSGVTACINIALVHHLG 6.3 278 0 5.4 ARG NH1 112 0 9.9 ASP OD2 102 0.79 0 -35.677 12.01 0 Nagahara, N. and Katayama, A. 2005. Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteinesulfenate in the maintenance of redox homeostasis. J Biol Chem. 280: 34569-34576. PMID: 16107337. 16107337 POSSIBLE 3-MERCAPTOPYRUVATE SULFURTRANSFERASE HOOH or tetrathionate SH LEISHMANIA MAJOR TRANSFERASE 2.8.1.2
1OKG A 278 HLGLGHPYLYCGSWSEYSGLF 6.3 260 0 3.4 ARG NH1 112 0 8.3 GLU OE2 283 2.2 0 -13.688 7.99 0 Nagahara, N. and Katayama, A. 2005. Post-translational regulation of mercaptopyruvate sulfurtransferase via a low redox potential cysteinesulfenate in the maintenance of redox homeostasis. J Biol Chem. 280: 34569-34576. PMID: 16107337. 16107337 POSSIBLE 3-MERCAPTOPYRUVATE SULFURTRANSFERASE HOOH or tetrathionate SH LEISHMANIA MAJOR TRANSFERASE 2.8.1.2
1OOA A 59 KQRGFRFRYVCEGPSHGGLPG 19.2 116 0 8.2 LYS NZ 146 31.38 5.4 GLU OE2 60 3.94 44 -25.976 10.44 0 1NFK NFKB SH MUS MUSCULUS TRANSCRIPTION/RNA N/A
1OOA A 116 LHAHSLVGKHCEDGVCTVTAG 4 121 1.4 8.9 HIS NE2 115 31.26 9.7 GLU OE1 117 30.65 0 -33.629 9.93 1 1NFK NFKB SS MUS MUSCULUS TRANSCRIPTION/RNA N/A
1OOA A 121 LVGKHCEDGVCTVTAGPKDMV 4 116 0 7.3 HIS NE2 115 31.26 10.8 GLU OE1 117 30.65 1 -22.271 12.42 1 1NFK NFKB SS MUS MUSCULUS TRANSCRIPTION/RNA N/A
1OOA A 259 KIVRMDRTAGCVTGGEEIYLL 25.2 270 0 8.5 LYS NZ 315 23.12 5.1 GLU OE2 264 19.98 11 -13.517 5.16 0 1NFK NFKB SH MUS MUSCULUS TRANSCRIPTION/RNA N/A
1ORB A 63 PGASFFDIEECRDKASPYEVM 13.5 254 0 7.6 LYS NZ 66 27.07 8.7 GLU OE2 62 15.47 1 -16.23 10.45 0 2ORA CARBOXYMETHYLATED RHODANESE SH BOS TAURUS TRANSFERASE 2.8.1.1
1ORB A 247 VDLTKPLIATCRKGVTACHIA 9.2 254 0 6.3 ARG NH2 186 10.03 4.4 ASP OD1 180 0 9 -11.199 7.73 1 2ORA CARBOXYMETHYLATED RHODANESE SS BOS TAURUS TRANSFERASE 2.8.1.1
1OY1 A 138 AHQAGKPLGFCIAPALPKIFD 13 176 1.97 12.1 HIS NE2 173 0 3.3 GLU OE2 24 0 16 -11.978 8.68 1 1VHQ  SIGMA CROSS-REACTING PROTEIN 27A SOH E-COLI/K12 UNKNOWN FUNCTION N/A
1OY1 A 176 VLEEGAEHVPCPVDDIVVDED 13 138 15.96 8.1 HIS NE2 173 0 4.7 ASP OD2 180 33.09 2 -30.03 9.52 0 1VHQ  SIGMA CROSS-REACTING PROTEIN 27A SH E-COLI/K12 UNKNOWN FUNCTION N/A
1P15 A 660 ITVELKKEEECESYTVRDLLV 18.6 619 0.39 9.4 ARG NH1 682 30.71 6.3 GLU OE2 661 0 31.8 -22.816 7.98 0 van der Wijk, T., Overvoorde, J., and den Hertog, J. 2004. H2O2-induced intermolecular disulfide bond formation between receptor protein-tyrosine phosphatases. J Biol Chem. 279: 44355-44361. PMID: 15294898. 15294898 PROTEIN-TYROSINE PHOSPHATASE ALPHA HOOH SH MUS MUSCULUS HYDROLASE 3.1.3.48
1P15 A 724 QSGNHPITVHCSAGAGRTGTF 8.6 635 0 7 ARG NH1 730 5.62 13.1 GLU OE2 626 4 4.8 1.797 -0.95 1 van der Wijk, T., Overvoorde, J., and den Hertog, J. 2004. H2O2-induced intermolecular disulfide bond formation between receptor protein-tyrosine phosphatases. J Biol Chem. 279: 44355-44361. PMID: 15294898. 15294898 PROTEIN-TYROSINE PHOSPHATASE ALPHA HOOH intermol SS MUS MUSCULUS HYDROLASE 3.1.3.48
1P15 A 735 SAGAGRTGTFCALSTVLERVK 9.4 724 4.76 10 ARG NH1 763 0 10.7 ASP OD2 587 2.16 0 -20.756 12.17 0 van der Wijk, T., Overvoorde, J., and den Hertog, J. 2004. H2O2-induced intermolecular disulfide bond formation between receptor protein-tyrosine phosphatases. J Biol Chem. 279: 44355-44361. PMID: 15294898. 15294898 PROTEIN-TYROSINE PHOSPHATASE ALPHA HOOH SH MUS MUSCULUS HYDROLASE 3.1.3.48
1PS4 A 46 AGLAGKDPVQCSRDVVICPDA 10.3 53 51.11 9.5 ARG NH1 48 14.82 4.8 GLU OE1 16 0 0 -39.659 8.74 0 1SOA DJ-1 HOOH SH HOMO SAPIENS RNA BINDING PROTEIN N/A
1PS4 A 53 PVQCSRDVVICPDASLEDAKK 10.3 46 0 6.1 LYS NZ 41 23.86 8.8 ASP OD1 55 25.54 51 -28.241 9 0 1SOA DJ-1 HOOH SH HOMO SAPIENS RNA BINDING PROTEIN N/A
1PS4 A 106 ENRKGLIAAICAGPTALLAHE 12.8 46 0 5.3 HIS NE2 126 28.32 3.1 GLU OE2 18 0 12 -30.074 10.46 1 1SOA DJ-1 HOOH SOOH HOMO SAPIENS RNA BINDING PROTEIN N/A
1PT1 A 26 THADLHYEGSCAIDQDFLDAA 11.7 78 32.64 11.3 HIS NE2 17 1.47 11.2 GLU OE2 40 11.93 0 -20.038 10.74 0 1PQF ASPARTATE DECARBOXYLASE SH E-COLI LYASE 4.1.1.11
1PT1 A 78 IISVNGAAAHCASVGDIVIIA 11.7 26 0 5.6 LYS NZ 53 27.22 9 ASP OD2 83 1.26 33 -19.732 9 1 1PQF ASPARTATE DECARBOXYLASE SOH E-COLI LYASE 4.1.1.11
1PVN A 26 LLIPGLSTVDCIPSNVNLSTP 5.6 459 0 7.6 LYS NZ  472 43.54 4 ASP OD1 25 8.67 3 -23.728 5.9 1 1LRT INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE SS TRITRICOMONAS FOETUS OXIDOREDUCTASE 1.1.1.205
1PVN A 356 FEETGIYIPVCSDGGIVYDYH 7.4 259 0 6.2 LYS NZ  310 1.8 5.7 ASP OD1 358 8.53 0 -22.697 13.03 0 1LRT INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE SH TRITRICOMONAS FOETUS OXIDOREDUCTASE 1.1.1.205
1PVN A 459 ASLNKVKSTMCNCGALTIPQL 5.6 26 3.31 9.3 LYS NZ  455 43.24 8.1 ASP OD1 25 8.67 0 -27.955 11.81 1 1LRT INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE SS TRITRICOMONAS FOETUS OXIDOREDUCTASE 1.1.1.205
1PVN A 461 LNKVKSTMCNCGALTIPQLQS 9.2 459 0 8.4 LYS NZ  474 28.13 13.4 ASP OD1 25 8.67 1 -36.505 11.79 0 1LRT INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE SH TRITRICOMONAS FOETUS OXIDOREDUCTASE 1.1.1.205
1QFS A 25 AIQDYHGHKVCDPYAWLEDPD 20.3 601 10.81 7 ARG NH2 11 27.33 6.2 GLU OE1 13 12.72 48 -29.312 9 1 1QFM PROLYL OLIGOPEPTIDASE SOH SUS SCROFA HYDROLASE 3.4.21.26
1QFS A 57 NKITVPFLEQCPIRGLYKERM 8.8 703 0 5.1 ARG NH1 702 0.76 9.5 ASP OD1 707 28.26 29 -40.261 9.05 1 1QFM PROLYL OLIGOPEPTIDASE SOH SUS SCROFA HYDROLASE 3.4.21.26
1QFS A 78 TELYDYPKYSCHFKKGKRYFY 11.9 352 0 8.9 ARG NH1 98 21.62 11.2 GLU OE1 393 6.49 0 -34.857 10.86 0 1QFM PROLYL OLIGOPEPTIDASE SH SUS SCROFA HYDROLASE 3.4.21.26
1QFS A 175 PDVLERVKFSCMAWTHDGKGM 9.9 225 0 11.8 ARG NH2 252 26.59 9.4 GLU OE1 239 11.74 0 -23.691 8.51 1 1QFM PROLYL OLIGOPEPTIDASE SOOH SUS SCROFA HYDROLASE 3.4.21.26
1QFS A 225 LGTDQSEDILCAEFPDEPKWM 8.6 264 0.75 11.7 LYS NZ 183 48.57 8 GLU OE1 269 8.96 0 -25.29 10.48 0 1QFM PROLYL OLIGOPEPTIDASE SH SUS SCROFA HYDROLASE 3.4.21.26
1QFS A 255 RYVLLSIREGCDPVNRLWYCD 13.6 601 10.81 8 ARG NH1 643 40.68 6.7 ASP OD1 598 0 29 -23.61 10.98 1 1QFM PROLYL OLIGOPEPTIDASE SOH SUS SCROFA HYDROLASE 3.4.21.26
1QFS A 526 KGGILANKQNCFDDFQCAAEY 9.3 563 0 3.3 LYS NZ 523 1.13 6 ASP OD2 529 0 0 -18.177 8.25 0 1QFM PROLYL OLIGOPEPTIDASE SH SUS SCROFA HYDROLASE 3.4.21.26
1QFS A 532 NKQNCFDDFQCAAEYLIKEGY 9.7 563 0 7.4 ARG NH1 567 15.76 3.8 GLU OE2 535 14.91 17 -20.345 8.48 0 1QFM PROLYL OLIGOPEPTIDASE SH SUS SCROFA HYDROLASE 3.4.21.26
1QFS A 601 IGHAWTTDYGCSDSKQHFEWL 13.6 255 28.85 4 HIS NE2 587 4.15 3.8 ASP OD2 603 30.52 11 -16.158 7.33 1 1QFM PROLYL OLIGOPEPTIDASE SOOH SUS SCROFA HYDROLASE 3.4.21.26
1QFS A 703 VSDMFAFIARCLNIDWIP--- 5.1 573 0 8 ARG NH1 702 0.76 12.3 ASP OD1 695 3.06 0 -19.25 9.63 0 1QFM PROLYL OLIGOPEPTIDASE SH SUS SCROFA HYDROLASE 3.4.21.26
1QLP A 232 KRLGMFNIQHCKKLSSWVLLM ? ? ? 7 LYS NZ  234 42.89 9 GLU OE1 266 22.46 19 -7.647 5.7 1 Griffiths, S.W., King, J., and Cooney, C.L. 2002. The reactivity and oxidation pathway of cysteine 232 in recombinant human alpha 1-antitrypsin. J. Biol. Chem. 277: 25486-25492. PMID: 11991955.   11991955 ALPHA-1-ANTITRYPSIN SOOOH HOMO SAPIENS SERINE PROTEASE INHIBITOR N/A
1R1R A 179 AQFLYILVAACLFSNYPRETR 21.1 225 3.3 3.9 HIS NE2 118 0 7 ASP OD2 116 6.38 0 -45.767 5.36 0 2RIR RIBONUCLEOTIDE REDUCTASE R1 PROTEIN SH E-COLI OXIDOREDUCTASE 1.17.4.1
1R1R A 225 VRTPTRQFSSCVLIECGDSLD 5.9 462 0 15.6 ARG NH1 251 37.08 5.7 GLU OE2 441 4.36 3 -17.828 9.09 1 2RIR RIBONUCLEOTIDE REDUCTASE R1 PROTEIN SS E-COLI OXIDOREDUCTASE 1.17.4.1
1R1R A 420 GRIYIQNVDHCNTHSPFDPAI 14.2 462 0 5.7 LYS NZ  727 2.16 7.1 ASP OD1 418 0 0 -43.632 10.2 0 2RIR RIBONUCLEOTIDE REDUCTASE R1 PROTEIN SH E-COLI OXIDOREDUCTASE 1.17.4.1
1R1R A 439 AIAPVRQSNLCLEIALPTKPL 8.3 225 3.3 8.5 ARG NH2 411 37.8 4.9 GLU OE1 441 0 33 -17.025 12.36 0 2RIR RIBONUCLEOTIDE REDUCTASE R1 PROTEIN SH E-COLI OXIDOREDUCTASE 1.17.4.1
1R1R A 462 VNDENGEIALCTLSAFNLGAI 5.9 225 3.3 12.5 LYS NZ  727 2.16 7.3 GLU OE2 441 4.36 0 -18.493 11.8 1 2RIR RIBONUCLEOTIDE REDUCTASE R1 PROTEIN SS E-COLI OXIDOREDUCTASE 1.17.4.1
1R1R A 565 SNELAKEQGACPWFNETTYAK 12.8 462 0 7.7 ARG NH1 612 11.54 8.1 ASP OD1 490 0 0 -15.705 8.55 0 2RIR RIBONUCLEOTIDE REDUCTASE R1 PROTEIN SH E-COLI OXIDOREDUCTASE 1.17.4.1
1RQA B 93 GTFATLSELHCDKLHVDPENF 27.5 112 59.96 5.1 HIS NE2 146 14.49 3.5 ASP OD1 94 4.25 14 -23.474 8.84 1 1RQ4 HUMAN HEMOGLOBIN NO SOH HOMO SAPIENS OXYGEN STORAGE/TRANSPORT N/A
1RTH A 38 EEKIKALVEICTEMEKEGKIS 50.3 280 45.35 6.5 LYS NZ 73 10.86 8.4 GLU OE1 42 0.05 0 -27.976 9.81 0 1EP4 HIV-1 REVERSE TRANSCRIPTASE SH HIV TYPE I TRANSFERASE 2.7.7.49
1RTH A 280 IYPGIKVRQLCKLLRGTKALT 50.3 38 0 8.7 LYS NZ 281 10.04 8 GLU OE1 302 0 45 -16.375 9 1 1EP4 HIV-1 REVERSE TRANSCRIPTASE SOOH HIV TYPE I TRANSFERASE 2.7.7.49
1RW7 A 138 YANGGVVAAVCHGPAIFDGLT ? ? ? 5.2 HIS NE2 139 0 3.2 GLU OE2 30 0 3 -20.658 7.59 1 1QVZ YDR533C SOH SACCAROMYCES CEREVICIAE UNKNOWN FUNCTION N/A
1TD2 A 53 NHTQYGKWTGCVMPPSHLTEI 17.1 122 16.34 9.1 HIS NE2 59 11.74 13.6 GLU OE1 62 29.83 35 -16.164 3.39 1 1VI9 PYRIDOXAMINE KINASE SOOH E-COLI TRANSFERASE 2.7.1.35
1TD2 A 76 GIAAIDKLHTCDAVLSGYLGS 15.2 111 0 10.8 LYS NZ 101 19.84 6.8 ASP OD1 77 3.64 0 -15.568 8.67 0 1VI9 PYRIDOXAMINE KINASE SH E-COLI TRANSFERASE 2.7.1.35
1TD2 A 111 KAANPQAKYFCDPVMGHPEKG 14.3 122 16.34 5.2 HIS NE2 132 0 7 ASP OD2 112 0 0 -17.552 7.23 0 1VI9 PYRIDOXAMINE KINASE SH E-COLI TRANSFERASE 2.7.1.35
1TD2 A 122 DPVMGHPEKGCIVAPGVAEFH 14.3 111 0 8.3 HIS NE2 44 0 7.1 ASP OD2 224 7.46 16 -17.272 10.44 0 1VI9 PYRIDOXAMINE KINASE SH E-COLI TRANSFERASE 2.7.1.35
1U8F O 152 NSLKIISNASCTTNCLAPLAK 9.8 156 0 5.9 HIS NE2 179 8.62 7.6 ASP OD1 315 0 20 -17.87 11.76 1 1J0X GAPDH HOOH SOH HOMO SAPIENS OXIDOREDUCTASE 1.2.1.12
1U8F O 156 IISNASCTTNCLAPLAKVIHD 9.8 152 19.84 9.4 HIS NE2 179 8.62 10.4 ASP OD1 289 0.16 0 -17.977 9.51 0 1J0X GAPDH SH HOMO SAPIENS OXIDOREDUCTASE 1.2.1.12
1U8F O 247 TANVSVVDLTCRLEKPAKYDD 13.2 156 0 9.7 LYS NZ 309 16.38 9 ASP OD2 244 0 0 -15.69 11.75 0 1J0X GAPDH SH HOMO SAPIENS OXIDOREDUCTASE 1.2.1.12
1U8F O 284 LGYTEHQVVSCDFNSDTHSST 16.6 156 0 13.1 HIS NE2 53 0 4.1 ASP OD1 285 27.14 35 -8.665 9.19 0 1J0X GAPDH SH HOMO SAPIENS OXIDOREDUCTASE 1.2.1.12
1UMJ A 29 KTLLKERLIACANLREHRAFY ? ? ? 3.5 LYS NZ 56 0 9 GLU OE1 99 25.52 9 -12.892 5 1 1V9B PYROCOCCUS HORIKOSHII CUTA  SOOH PYROCOCCUS HORIKOSHII UNKNOWN FUNCTION N/A
1UTR A 5 ---------ICPGFLQVLEAL 20 71 58.42 16.2 LYS NZ 60 43.65 10.3 GLU OE1 63 27.9 77 -32.256 9 1 2UTG UTEROGLOBIN-PCB COMPLEX SS RATTUS NORVEGICUS MAMMALIAN PCB BINDING PROTEIN N/A
1UTR A 71 LTEKILTSPLC---------- 20 5 77.04 11.3 LYS NZ 64 27.13 16.1 GLU OE1 63 27.9 58 -26.094 8.69 1 2UTG UTEROGLOBIN-PCB COMPLEX SS RATTUS NORVEGICUS MAMMALIAN PCB BINDING PROTEIN N/A
1VH2 A 82 EGVVDVSPMGCRTGMYMAVIG 20.6 125 2.2 3.8 ARG NH1 42 1.37 7.4 ASP OD1 40 0 15 -22.979 2.2 1 1VGX S-RIBOSYLHOMOCYSTEINASE SOOH DEINOCOCCUS RADIODURANS HYDROLASE 3.13.1.-
1VH2 A 125 QPIPGVSELECGNYRDHDLAA 20.6 82 14.88 3.4 HIS NE2 57 8.98 6.6 GLU OE1 60 10.89 2 -17.714 2.21 0 1VGX S-RIBOSYLHOMOCYSTEINASE SH DEINOCOCCUS RADIODURANS HYDROLASE 3.13.1.-
1X9E A 111 FARSFEIKEACYGATAGLQLA ? ? ? 3.6 HIS NE2 233 4.28 3.8 GLU OE2 79 0 7 -29.458 8.33 1 1YSL HMG-COA SYNTHASE SOOH ENTEROCOCCUS FAECALIS LYASE 4.1.3.5
1XJN A 134 SRNHLHMLSACFVVPVGDSIE 5.7 333 0 10.4 ARG NH1 388 4.87 4.4 GLU OE2 324 4.26 2 -20.329 15.18 1 1XJF RIBONUCLEOTIDE REDUCTASE, B12-DEPENDENT SS THERMOTOGA MARITIMA OXIDOREDUCTASE 1.17.4.1
1XJN A 322 PHRKINSTNPCGEIGLSDYEA 7.9 134 1.64 11.8 LYS NZ  229 10.79 4.8 GLU OE1 324 0 47 -12.904 12.64 0 1XJF RIBONUCLEOTIDE REDUCTASE, B12-DEPENDENT SH THERMOTOGA MARITIMA OXIDOREDUCTASE 1.17.4.1
1XJN A 333 GEIGLSDYEACNLGSIDVAKF 5.7 134 1.64 6.4 ARG NH1 388 4.87 6.7 GLU OE2 331 0.2 0 -21.955 12.29 1 1XJF RIBONUCLEOTIDE REDUCTASE, B12-DEPENDENT SS THERMOTOGA MARITIMA OXIDOREDUCTASE 1.17.4.1
1XW3 A 99 GGDYFYSFGGCHRYAAYQQLQ ? ? ? 3.5 ARG NH2 51 3.6 11.5 ASP OD2 80 41.81 16 -8.082 4.98 1 1XW4 SULFIREDOXIN SOOH HOMO SAPIENS OXIDOREDUCTASE 1
1XWW A 12 EQATKSVLFVCLGNICRSPIA 7 17 1.88 5.1 ARG NH2 18 4.48 7.7 ASP OD1 129 2.98 2.2 1.382 1.42 1 Caselli, A., Marzocchini, R., Camici, G., Manao, G., Moneti, G., Pieraccini, G., and Ramponi, G. 1998. The inactivation mechanism of low molecular weight phosphotyrosine-protein phosphatase by H2O2. J Biol Chem. 273: 32554-32560. PMID: 9829991. 9829991 LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE               HOOH SS HOMO SAPIENS HYDROLASE 3.1.3.48, 3.1.3.2
1XWW A 17 SVLFVCLGNICRSPIAEAVFR 7 12 2.19 4.7 ARG NH2 58 4.99 4.3 ASP OD2 56 9.9 1.9 -38.848 10.64 1 Caselli, A., Marzocchini, R., Camici, G., Manao, G., Moneti, G., Pieraccini, G., and Ramponi, G. 1998. The inactivation mechanism of low molecular weight phosphotyrosine-protein phosphatase by H2O2. J Biol Chem. 273: 32554-32560. PMID: 9829991. 9829991 LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE               HOOH SS HOMO SAPIENS HYDROLASE 3.1.3.48, 3.1.3.2
1XWW A 62 GRSPDPRAVSCLRNHGIHTAH 8.9 145 0 4.5 HIS NE2 66 0.94 3.9 GLU OE1 139 5.08 1.1 -18.31 9.39 0 Caselli, A., Marzocchini, R., Camici, G., Manao, G., Moneti, G., Pieraccini, G., and Ramponi, G. 1998. The inactivation mechanism of low molecular weight phosphotyrosine-protein phosphatase by H2O2. J Biol Chem. 273: 32554-32560. PMID: 9829991. 9829991 LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE               HOOH SH HOMO SAPIENS HYDROLASE 3.1.3.48, 3.1.3.2
1XWW A 109 LNRKSNQVKTCKAKIELLGSY 12.2 90 0 10.4 LYS NZ  110 28.71 10.9 ASP OD1 86 17.94 8.7 -21.272 8.5 0 Caselli, A., Marzocchini, R., Camici, G., Manao, G., Moneti, G., Pieraccini, G., and Ramponi, G. 1998. The inactivation mechanism of low molecular weight phosphotyrosine-protein phosphatase by H2O2. J Biol Chem. 273: 32554-32560. PMID: 9829991. 9829991 LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE               HOOH SH HOMO SAPIENS HYDROLASE 3.1.3.48, 3.1.3.2
1XWW A 149 ETVYQQCVRCCRAFLEKAH-- 5.6 145 0 10.2 ARG NH2 150 48.9 10.5 GLU OE1 23 0.02 0 -29.844 11.71 0 Caselli, A., Marzocchini, R., Camici, G., Manao, G., Moneti, G., Pieraccini, G., and Ramponi, G. 1998. The inactivation mechanism of low molecular weight phosphotyrosine-protein phosphatase by H2O2. J Biol Chem. 273: 32554-32560. PMID: 9829991. 9829991 LOW MOLECULAR WEIGHT PHOSPHOTYROSINE PROTEIN PHOSPHATASE               HOOH SH HOMO SAPIENS HYDROLASE 3.1.3.48, 3.1.3.2
1XXU A 45 VFFPLAFTGICQGELDQLRDH ? ? ? 6.8 ARG NH2 139 0.27 5.8 GLU OE2 48 0 0 -19.089 7.17 1 1XVW AHPE SOH MYCOBACTRIUM TUBERCULOSIS OXIDOREDUCTASE 1.11.1.7
1Y1I X 336 DRVKKGGSYMCHRSYCYRYRC 3.4 341 11.96 6.7 ARG NH1 343 16.7 10.1 ASP OD2 111 0 1.3 -27.898 10.29 1 Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., von Figura, K., Ficner, R., and Rudolph, M.G. 2005. Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. Cell 121: 541-552. PMID: 15907468. 15907468 C-ALPHA-FORMYGLYCINE-GENERATING ENZYME SS, SOOOH HOMO SAPIENS OXIDOREDUCTASE 1
1Y1I X 341 GGSYMCHRSYCYRYRCAARSQ 3.4 336 1.26 3.8 ARG NH1 343 16.7 8 ASP OD2 111 0 12 -15.412 6.08 1 Dierks, T., Dickmanns, A., Preusser-Kunze, A., Schmidt, B., Mariappan, M., von Figura, K., Ficner, R., and Rudolph, M.G. 2005. Molecular basis for multiple sulfatase deficiency and mechanism for formylglycine generation of the human formylglycine-generating enzyme. Cell 121: 541-552. PMID: 15907468. 15907468 C-ALPHA-FORMYGLYCINE-GENERATING ENZYME SS, SOOOH HOMO SAPIENS OXIDOREDUCTASE 1
1Y25 A 80 RAAASGATVLCVSKDLPFAQK 6.6 93 3 10.2 ARG NH1 130 0.04 7.5 ASP OD1 68 0 0 -14.995 10.77 1 1XVQ MYCOBACTERIAL THIOL PEROXIDASE TPX SOH MYCOBACTRIUM TUBERCULOSIS OXIDOREDUCTASE 1.11.1.-
1Y25 A 93 KDLPFAQKRFCGAEGTENVMP 6.6 80 0 8.9 ARG NH2 91 21.58 7 ASP OD1 68 0 3 -30.194 7.86 0 1XVQ MYCOBACTERIAL THIOL PEROXIDASE TPX SH MYCOBACTRIUM TUBERCULOSIS OXIDOREDUCTASE 1.11.1.-
1Y8B A 271 VEAAISTILDCEDSVAAVDAE 17.9 617 12.97 8.6 ARG NH2 338 3.33 4.6 ASP OD1 363 2.94 17.5 -6.199 7.9 0 Anstrom, D.M., Kallio, K., and Remington, S.J. 2003. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 Å resolution. Protein Sci. 12: 1822-1832. PMID: 12930982. 12930982 MALATE SYNTHASE G O2 SH ESCHERICHIA COLI                                 TRANSFERASE 2.3.3.9
1Y8B A 496 ERNNVLSGLFCGLRGKAQIGK 9.3 438 1.69 6.8 ARG NH1 436 0.07 6.7 GLU OE2 427 0 3.1 -24.037 9.08 0 Anstrom, D.M., Kallio, K., and Remington, S.J. 2003. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 Å resolution. Protein Sci. 12: 1822-1832. PMID: 12930982. 12930982 MALATE SYNTHASE G O2 SH ESCHERICHIA COLI                                 TRANSFERASE 2.3.3.9
1Y8B A 617 VVRWVEQGIGCSKVPDIHNVA 17.9 271 17.53 11.8 ARG NH2 311 12.87 8.6 ASP OD2 631 2.52 13 -32.251 7.52 1 Anstrom, D.M., Kallio, K., and Remington, S.J. 2003. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 Å resolution. Protein Sci. 12: 1822-1832. PMID: 12930982. 12930982 MALATE SYNTHASE G O2 SOH ESCHERICHIA COLI                                 TRANSFERASE 2.3.3.9
1Y8B A 688 RPMAGNFANSCAFKAASDLIF 26 271 17.53 5 HIS NE2 723 6.55 7.9 GLU OE1 719 10.45 58.1 -17.223 8.71 1 Anstrom, D.M., Kallio, K., and Remington, S.J. 2003. Structure of the Escherichia coli malate synthase G:pyruvate:acetyl-coenzyme A abortive ternary complex at 1.95 Å resolution. Protein Sci. 12: 1822-1832. PMID: 12930982. 12930982 MALATE SYNTHASE G O2 SOH ESCHERICHIA COLI                                 TRANSFERASE 2.3.3.9
1YAF A 7 -----KFSEECRSAAAEWWEG 15.9 135 17.05 5.7 LYS NZ 195 19.73 6.1 GLU OE2 6 16.05 0 -31.66 10.27 0 1TO9 TENA FROM BACILLUS SUBTILIS SH BACILLUS SUBTILIS TRANSCRIPTION N/A
1YAF A 149 YYEVGEKLLHCDPGHPIYQKW 20.5 135 17.05 9.3 HIS NE2 148 31.74 8 ASP OD2 29 23.75 28 -31.203 8.7 1 1TO9 TENA FROM BACILLUS SUBTILIS SOOH BACILLUS SUBTILIS TRANSCRIPTION N/A
1YJQ A 8 ---MKITVLGCGALGQLWLTA 4.1 37 0 8.8 ARG NH2 124 20.52 13.6 GLU OE2 51 33.65 0 -23.617 10.52 1 1KS9 2-DEHYDROPANTOATE 2-REDUCTASE SS E-COLI OXIDOREDUCTASE 1.1.1.169
1YJQ A 37 QGWLRVPQPYCSVNLVETDGS 4.1 8 0 10.6 ARG NH2 124 20.52 9.8 GLU OE2 51 33.65 0 -22.98 7.63 1 1KS9 2-DEHYDROPANTOATE 2-REDUCTASE SS E-COLI OXIDOREDUCTASE 1.1.1.169
1YJQ A 181 AELWRKLAVNCVINPLTAIWN 9.3 208 0.2 10.4 ARG NH2 266 3.05 8.4 GLU OE1 210 0 0 -37.068 12.19 0 1KS9 2-DEHYDROPANTOATE 2-REDUCTASE SH E-COLI OXIDOREDUCTASE 1.1.1.169
1Z97 A 66 AKTILNNGKTCRVVFDDTYDR 15 183 8.53 9.3 HIS NE2 94 8.58 11.6 ASP OD2 165 3.88 0 -28.198 11.07 0 1FLJ CARBONIC ANHYDRASE III SH HOMO SAPIENS LYASE 4.2.1.1
1Z97 A 183 EAPFTKFDPSCLFPACRDYWT 15 66 0 9.9 ARG NH2 189 34.69 5.6 ASP OD1 180 0 9 -16.095 10.2 1 1FLJ CARBONIC ANHYDRASE III GSSG SSG HOMO SAPIENS LYASE 4.2.1.1
1Z97 A 188 KFDPSCLFPACRDYWTYQGSL 17.1 183 8.53 4.3 LYS NZ 213 25.27 3.6 ASP OD1 190 14.39 9 -9.84 7.3 1 1FLJ CARBONIC ANHYDRASE III GSSG SSG HOMO SAPIENS LYASE 4.2.1.1
1ZDL A 54 VIGGGSGGLACAKEAAQLGKK 16.4 86 12.54 8.3 ARG NH2 381 0 9.1 GLU OE2 347 0 0 -25.143 11.31 0 1ZKQ THIOREDOXIN REDUCTASE 2, MITOCHONDRIAL SH MUS MUSCULUS OXIDOREDUCTASE 1.8.1.9
1ZDL A 86 RGTKWGLGGTCVNVGCIPKKL 3.2 91 27.51 7 HIS NE2 143 6.2 10 ASP OD1 359 7.48 13 -13.083 9.97 1 1ZKQ THIOREDOXIN REDUCTASE 2, MITOCHONDRIAL SS MUS MUSCULUS OXIDOREDUCTASE 1.8.1.9
1ZDL A 91 GLGGTCVNVGCIPKKLMHQAA 3.2 86 12.54 6 LYS NZ  94 19.76 8.7 GLU OE1 232 10.75 28 -4.271 7.43 1 1ZKQ THIOREDOXIN REDUCTASE 2, MITOCHONDRIAL SS MUS MUSCULUS OXIDOREDUCTASE 1.8.1.9
1ZDL A 233 VVGASYVALECAGFLTGIGLD 12.2 91 27.51 8.6 LYS NZ  94 19.76 6.1 GLU OE1 232 10.75 5 -18.22 11.74 0 1ZKQ THIOREDOXIN REDUCTASE 2, MITOCHONDRIAL SH MUS MUSCULUS OXIDOREDUCTASE 1.8.1.9
1ZDL A 407 TTVFTPLEYGCVGLSEEEAVA 15.4 452 0 5.9 HIS NE2 464 0 7.9 GLU OE1 414 3.46 11 -18.645 10.42 0 1ZKQ THIOREDOXIN REDUCTASE 2, MITOCHONDRIAL SH MUS MUSCULUS OXIDOREDUCTASE 1.8.1.9
1ZDL A 446 FTVADRDASQCYIKMVCMREP 6.7 500 7.72 7.1 HIS NE2 267 5.16 7.5 ASP OD1 442 6.91 0 -26.456 10.29 0 1ZKQ THIOREDOXIN REDUCTASE 2, MITOCHONDRIAL SH MUS MUSCULUS OXIDOREDUCTASE 1.8.1.9
1ZDL A 500 VMQTVGIHPTCSEEVVKLHIS 6.7 446 0.25 10.4 LYS NZ  506 15.65 4.7 GLU OE1 435 15.66 8 -12.002 9.81 0 1ZKQ THIOREDOXIN REDUCTASE 2, MITOCHONDRIAL SH MUS MUSCULUS OXIDOREDUCTASE 1.8.1.9
1ZI6 A 60 WLVDQGYAAVCPDLYARQAPG 13.2 123 7.23 12 ARG NH1 45 23.93 7.9 ASP OD1 62 0.37 0 -30.542 11.75 0 1DIN DIENELACTONE HYDROLASE SH PSEODOMONAS PUTIDA HYDROLASE 3.1.1.45
1ZI6 A 123 SNGKVGLVGYCLGGALAFLVA 13.2 60 0 2.8 HIS NE2 202 0.62 5.7 GLU OE2 36 0.65 7 -36.241 4.82 1 1DIN DIENELACTONE HYDROLASE SOOH PSEODOMONAS PUTIDA HYDROLASE 3.1.1.45
1ZVQ A 51 RKQVVIDGETCLLDILDTAGG 20.6 80 0.25 4.6 ARG NH2 164 0.27 4.1 GLU OE1 49 0 0 -43.635 8.15 0 1XJ0 P21/H-RAS-1 SH HOMO SAPIENS ONCOPROTEIN N/A
1ZVQ A 118 DVPMVLVGNKCDLAARTVESR 17.8 80 0.25 6.6 ARG NH1 123 20.57 4.9 GLU OE2 143 12.03 6 -16.911 8.72 1 1XJ0 P21/H-RAS-1 SOH HOMO SAPIENS ONCOPROTEIN N/A
2AE2 A 10 --AGRWNLEGCTALVTGGSRG 8 236 0 3.8 ARG NH2 138 0 8.5 GLU OE1 8 19.05 8 -20.451 6.89 0 2AE1 TROPINONE REDUCTASE-II  SH HOMO SAPIENS SERINE PROTEASE INHIBITOR N/A
2AE2 A 39 LASLGASVYTCSRNQKELNDC 5 65 0.15 10.3 ARG NH2 41 36.48 8.7 GLU OE1 72 12.59 0 -11.323 8.95 1 2AE1 TROPINONE REDUCTASE-II  SS HOMO SAPIENS SERINE PROTEASE INHIBITOR N/A
2AE2 A 65 SKGFKVEASVCDLSSRSERQE 5 39 0.11 8.2 ARG NH1 73 1.19 4.3 GLU OE1 72 12.59 0 -20.902 11.46 1 2AE1 TROPINONE REDUCTASE-II  SS HOMO SAPIENS SERINE PROTEASE INHIBITOR N/A
2AE2 A 217 KENLNKLIDRCALRRMGEPKE 15.4 258 68.35 8 ARG NH1 221 2.05 7.3 ASP OD1 251 7.72 5 -28.268 4.94 0 2AE1 TROPINONE REDUCTASE-II  SH HOMO SAPIENS SERINE PROTEASE INHIBITOR N/A
2AE2 A 236 KELAAMVAFLCFPAASYVTGQ 8 10 7.53 6.5 ARG NH2 183 0.07 11.1 GLU OE1 28 22.47 0 -29.364 11.63 0 2AE1 TROPINONE REDUCTASE-II  SH HOMO SAPIENS SERINE PROTEASE INHIBITOR N/A
2AE2 A 258 IYVDGGLMANCGF-------- 15.4 217 4.55 9.5 ARG NH1 216 44.21 12.8 ASP OD2 215 26.3 68 -28.614 9 0 2AE1 TROPINONE REDUCTASE-II  SH HOMO SAPIENS SERINE PROTEASE INHIBITOR N/A
2AF3 C 159 SAFFIISVPDCEYGSDGTFLF 20 277 30.14 13 LYS NZ 203 7.16 7.3 GLU OE2 160 30.43 14 -13.183 7.93 1 2AF4 PHOSPHATE ACETYLTRANSFERASE SOH METHANOSACRINA THERMOPHILA TRANSFERASE 2.3.1.8
2AF3 C 312 AKPINDLSRGCSDEDIVGAVA 16.4 325 0.16 3.6 ARG NH1 28 5.54 5.2 ASP OD1 316 14.31 0 -28.932 10.56 0 2AF4 PHOSPHATE ACETYLTRANSFERASE SH METHANOSACRINA THERMOPHILA TRANSFERASE 2.3.1.8
2AF3 C 325 EDIVGAVAITCVQAAAQDK-- 16.4 312 0 8.2 LYS NZ 17 8.8 6.6 ASP OD2 118 4.8 0 -30.852 10.65 0 2AF4 PHOSPHATE ACETYLTRANSFERASE SH METHANOSACRINA THERMOPHILA TRANSFERASE 2.3.1.8
2AI9 A 110 QEAYLPTGEGCLSVDDNVAGL ? ? ? 3.8 HIS NE2 157 0.07 6.8 GLU OE2 154 4.89 0 -16.908 -3.8 1 1Q1Y PEPTIDE DEFORMYLASE PDF1 SOOH STAPHYLOCOCCUS AUREUS HYDROLASE 3.5.1.88
2B3Z A 74 GADIYVTLEPCSHYGKTPPCA 3.9 83 3.33 5 HIS NE2 49 29.47 5.5 GLU OE2 51 4.85 5 -29.667 2.77 1 2D5N RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBD SS BACILLUS SUBTILIS HYDROLASE/OXIDOREDUCTASE 3.5.4.26/1.1.1.193
2B3Z A 83 PCSHYGKTPPCAELIINSGIK 3.9 74 5.03 5.8 HIS NE2 49 29.47 3.8 GLU OE1 51 0.92 3 -21.867 9.38 1 2D5N RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBD SS BACILLUS SUBTILIS HYDROLASE/OXIDOREDUCTASE 3.5.4.26/1.1.1.193
2B3Z A 233 LSIPEDAKVICDQIAPTWIFT 21.2 205 0.88 9.1 ARG NH2 216 1.27 6.5 ASP OD1 228 12.37 14 -20.846 9.07 0 2D5N RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBD SH BACILLUS SUBTILIS HYDROLASE/OXIDOREDUCTASE 3.5.4.26/1.1.1.193
2B3Z A 304 AVHGSFVKEGCFQEIIFYFAP 25 205 0.88 9 HIS NE2 139 2.69 5.9 GLU OE1 302 30.1 12 -26.103 9.68 0 2D5N RIBOFLAVIN BIOSYNTHESIS PROTEIN RIBD SH BACILLUS SUBTILIS HYDROLASE/OXIDOREDUCTASE 3.5.4.26/1.1.1.193
2B4E A 24 VFGQPAKADQCYEDVRVSQTT 7.4 345 0 5.7 LYS NZ 344 37.16 4.5 GLU OE1 26 3.45 4 -20.881 10.36 0 2AQ5 MURINE CORONIN-1 SH MUS MUSCULUS STRUCTURAL PROTEIN N/A
2B4E A 51 AVNPKFMALICEASGGGAFLV 9.3 78 8.37 5.3 ARG NH2 29 22.19 8.8 GLU OE1 52 3.29 5 -9.748 9.93 0 2AQ5 MURINE CORONIN-1 SH MUS MUSCULUS STRUCTURAL PROTEIN N/A
2B4E A 78 GRVDKNVPLVCGHTAPVLDIA 9.3 51 4.88 4.2 ARG NH2 121 46.41 11.2 ASP OD2 103 0.6 8 -29.51 7.42 1 2AQ5 MURINE CORONIN-1 SOH MUS MUSCULUS STRUCTURAL PROTEIN N/A
2B4E A 90 HTAPVLDIAWCPHNDNVIASG 17.4 40 0 6.6 HIS NE2 92 1.33 7.5 ASP OD1 94 1.64 8 -30.668 7.86 1 2AQ5 MURINE CORONIN-1 SOH MUS MUSCULUS STRUCTURAL PROTEIN N/A
2B4E A 104 DNVIASGSEDCTVMVWEIPDG 9.2 152 16.65 8.5 LYS NZ 132 38.57 6.2 ASP OD1 103 0 26 -48.106 9.14 0 2AQ5 MURINE CORONIN-1 SH MUS MUSCULUS STRUCTURAL PROTEIN N/A
2B4E A 152 TAQNVLLSAGCDNVILVWDVG 9.2 104 25.62 4.9 ARG NH2 133 31.97 7.3 ASP OD1 153 0 17 -22.533 8.75 1 2AQ5 MURINE CORONIN-1 SOH MUS MUSCULUS STRUCTURAL PROTEIN N/A
2B4E A 192 VDWSRDGALICTSCRDKRVRV 11.7 195 0 8.8 HIS NE2 175 0 6.4 ASP OD2 183 4.53 0 -20.597 11.54 0 2AQ5 MURINE CORONIN-1 SH MUS MUSCULUS STRUCTURAL PROTEIN N/A
2B4E A 195 SRDGALICTSCRDKRVRVIEP 11.3 152 16.65 3.9 ARG NH1 201 0 3.1 ASP OD1 197 0 0 -20.722 3.19 0 2AQ5 MURINE CORONIN-1 SH MUS MUSCULUS STRUCTURAL PROTEIN N/A
2B4E A 285 FDPDTNIVYLCGKGDSSIRYF 11.1 40 0 9.2 ARG NH1 293 2.05 7.7 ASP OD2 289 0.64 0 -21.968 11.66 0 2AQ5 MURINE CORONIN-1 SH MUS MUSCULUS STRUCTURAL PROTEIN N/A
2B4E A 332 MPKRGLEVNKCEIARFYKLHE 21.8 285 0.02 5.9 ARG NH1 354 3.44 7.8 ASP OD2 362 0 11 -20.742 9 1 2AQ5 MURINE CORONIN-1 SOH MUS MUSCULUS STRUCTURAL PROTEIN N/A
2B5E A 406 DVLVLYYAPWCGHCKRLAPTY 3.2 409 0 7.5 HIS NE2 408 18.05 10.2 ASP OD2 436 0 12 -27.466 5.02 1 Grillo, C., D'Ambrosio, C., Consalvi, V., Chiaraluce, R., Scaloni, A., Maceroni, M., Eufemi, M., and Altieri, F. 2007. DNA-binding activity of the ERp57 C-terminal domain is related to a redox-dependent conformational change. J Biol Chem. 282:10299-10310. PMID: 17283067. 17283067 PROTEIN DISULFIDE-ISOMERASE  SS SACCAROMYCES CEREVICIAE ISOMERASE 5.3.4.1
2B5E A 409 VLYYAPWCGHCKRLAPTYQEL 3.2 406 12.18 7.5 ARG NH1 471 6.4 9 ASP OD2 436 0 0 -16.17 8.35 1 Grillo, C., D'Ambrosio, C., Consalvi, V., Chiaraluce, R., Scaloni, A., Maceroni, M., Eufemi, M., and Altieri, F. 2007. DNA-binding activity of the ERp57 C-terminal domain is related to a redox-dependent conformational change. J Biol Chem. 282:10299-10310. PMID: 17283067. 17283067 PROTEIN DISULFIDE-ISOMERASE  SS SACCAROMYCES CEREVICIAE ISOMERASE 5.3.4.1
2B5H A 93 SSIHDHTDSHCFLKLLQGNLK 9.1 130 0 3.7 HIS NE2 88 0.02 7.8 GLU OE2 104 1.72 0.2 -33.672 0.28 0 Joseph, C.A. and Maroney, M.J. 2007. Cysteine dioxygenase: structure and mechanism. Chem. Commun. 3338–3349. CYSTEINE DIOXYGENASE TYPE I O2 SH RATTUS NORVEGICUS OXIDOREDUCTASE 1.13.11.20
2B5H A 130 KSERTLRENQCAYINDSIGLH 9.1 93 0.24 6.9 LYS NZ  96 0 5.6 GLU OE1 38 5.77 0 -17.277 10.42 0 Joseph, C.A. and Maroney, M.J. 2007. Cysteine dioxygenase: structure and mechanism. Chem. Commun. 3338–3349. CYSTEINE DIOXYGENASE TYPE I O2 SH RATTUS NORVEGICUS OXIDOREDUCTASE 1.13.11.20
2B5H A 164 LHLYSPPFDTCHAFDQRTGHK 9.5 93 0.24 6.5 HIS NE2 86 8.54 4.5 ASP OD1 87 0 8 -13.433 11.15 1 Joseph, C.A. and Maroney, M.J. 2007. Cysteine dioxygenase: structure and mechanism. Chem. Commun. 3338–3349. CYSTEINE DIOXYGENASE TYPE I O2 intermol SS RATTUS NORVEGICUS OXIDOREDUCTASE 1.13.11.20
2BTF A 217 EIVRDIKEKLCYVALDFEQEM 4.2 257 0 8 ARG NH2 254 6.61 9.1 GLU OE1 253 0.04 0.4 -19.866 10.69 0 Lassing, I., Schmitzberger, F., Björnstedt, M., Holmgren, A., Nordlund, P., Schutt, C.E., and Lindberg, U. 2007. Molecular and structural basis for redox regulation of beta-actin. J Mol Biol. 370: 331-48. PMID: 17521670. 17521670 BETA-ACTIN HOOH SH BOS TAURUS BETA-ACTIN N/A
2BTF A 257 VITIGNERFRCPEALFQPSFL 4.2 217 0.4 6.8 LYS NZ  213 9.24 9.8 ASP OD1 187 0.37 0 -24.107 13.32 0 Lassing, I., Schmitzberger, F., Björnstedt, M., Holmgren, A., Nordlund, P., Schutt, C.E., and Lindberg, U. 2007. Molecular and structural basis for redox regulation of beta-actin. J Mol Biol. 370: 331-48. PMID: 17521670. 17521670 BETA-ACTIN HOOH SH BOS TAURUS BETA-ACTIN N/A
2BTF A 272 FQPSFLGMESCGIHETTFNSI 16.2 285 0 7.9 HIS NE2 275 18.11 4.1 GLU OE2 276 28.47 48.6 -23.964 8.74 1 Lassing, I., Schmitzberger, F., Björnstedt, M., Holmgren, A., Nordlund, P., Schutt, C.E., and Lindberg, U. 2007. Molecular and structural basis for redox regulation of beta-actin. J Mol Biol. 370: 331-48. PMID: 17521670. 17521670 BETA-ACTIN HOOH SS, SOOH BOS TAURUS BETA-ACTIN N/A
2BTF A 285 HETTFNSIMKCDVDIRKDLYA 16.2 272 48.6 5.2 HIS NE2 173 9.65 8.7 ASP OD2 286 40.65 0 -14.848 10.95 0 Lassing, I., Schmitzberger, F., Björnstedt, M., Holmgren, A., Nordlund, P., Schutt, C.E., and Lindberg, U. 2007. Molecular and structural basis for redox regulation of beta-actin. J Mol Biol. 370: 331-48. PMID: 17521670. 17521670 BETA-ACTIN HOOH SH BOS TAURUS BETA-ACTIN N/A
2BTF A 374 ESGPSIVHRKCF--------- 19.1 17 0.53 5.1 ARG NH1 116 0.86 7 GLU OE2 107 3.73 0 -20.045 8.64 1 Lassing, I., Schmitzberger, F., Björnstedt, M., Holmgren, A., Nordlund, P., Schutt, C.E., and Lindberg, U. 2007. Molecular and structural basis for redox regulation of beta-actin. J Mol Biol. 370: 331-48. PMID: 17521670. 17521670 BETA-ACTIN HOOH SS BOS TAURUS BETA-ACTIN N/A
2BXS A 201 ALWFLWYVKQCGGTTRIFSVT 14.6 406 8.81 8.6 LYS NZ  440 2.07 10 GLU OE1 450 0 0 -25.489 11.23 0 2BXR AMINE OXIDASE [FLAVIN-CONTAINING] A SH HOMO SAPIENS OXIDOREDUCTASE 1.4.3.4
2BXS A 266 IETLNHEHYECKYVINAIPPT 28 406 8.81 6.7 ARG NH2 429 0.17 8.8 ASP OD1 15 21.71 0 -15.802 7.92 0 2BXR AMINE OXIDASE [FLAVIN-CONTAINING] A SH HOMO SAPIENS OXIDOREDUCTASE 1.4.3.4
2BXS A 321 KEAFWKKKDYCGCMIIEDEDA 4.6 323 8.62 7 LYS NZ  316 1.44 5.1 GLU OE1 95 0 0 -30.403 10.2 1 2BXR AMINE OXIDASE [FLAVIN-CONTAINING] A SS HOMO SAPIENS OXIDOREDUCTASE 1.4.3.4
2BXS A 323 AFWKKKDYCGCMIIEDEDAPI 4.6 321 0 10.9 LYS NZ  316 1.44 9.5 GLU OE2 216 24.3 9 -25.041 13.08 1 2BXR AMINE OXIDASE [FLAVIN-CONTAINING] A SS HOMO SAPIENS OXIDOREDUCTASE 1.4.3.4
2BXS A 374 LHKEIRKKKICELYAKVLGSQ 10.1 306 0 7.1 LYS NZ  370 29.06 8.3 GLU OE1 375 15.97 1 -31 9.67 0 2BXR AMINE OXIDASE [FLAVIN-CONTAINING] A SH HOMO SAPIENS OXIDOREDUCTASE 1.4.3.4
2BXS A 398 HPVHYEEKNWCEEQYSGGCYT 9.5 406 8.81 8.6 ARG NH2 369 10.05 3.9 ASP OD1 359 17.07 1 -17.656 10.02 0 2BXR AMINE OXIDASE [FLAVIN-CONTAINING] A SH HOMO SAPIENS OXIDOREDUCTASE 1.4.3.4
2BXS A 406 NWCEEQYSGGCYTAYFPPGIM 9.5 398 1.15 6.4 ARG NH1 51 1.48 9.1 GLU OE1 436 0 9 -24.168 10.83 0 2BXR AMINE OXIDASE [FLAVIN-CONTAINING] A SH HOMO SAPIENS OXIDOREDUCTASE 1.4.3.4
2BZN A 68 VGTFEMAKVLCKFSLFTAVHK 4 95 13.92 8.2 HIS NE2 98 1.86 8.8 GLU OE1 97 25.69 4 -27.18 10.04 1 2A7R GMP REDUCTASE 2 SS HOMO SAPIENS OXIDOREDUCTASE 1.7.1.7
2BZN A 95 WQEFAGQNPDCLEHLAASSGT 4 68 4.02 7.4 LYS NZ  69 21.98 7.3 ASP OD2 94 39.22 14 -14.484 9 1 2A7R GMP REDUCTASE 2 SS HOMO SAPIENS OXIDOREDUCTASE 1.7.1.7
2BZN A 127 LEAIPQVKYICLDVANGYSEH 15.5 186 16.57 5 LYS NZ  177 2.8 3.3 ASP OD2 129 0 0 -44.132 13.14 0 2A7R GMP REDUCTASE 2 SH HOMO SAPIENS OXIDOREDUCTASE 1.7.1.7
2BZN A 186 IKVGIGPGSVCTTRKKTGVGY 14.4 222 0.34 7.1 ARG NH1 189 0 5.9 GLU OE1 289 5.83 17 -11.05 5.78 0 2A7R GMP REDUCTASE 2 SH HOMO SAPIENS OXIDOREDUCTASE 1.7.1.7
2BZN A 205 GYPQLSAVMECADAAHGLKGH 14.7 222 0.34 10.2 HIS NE2 210 0.3 5.5 GLU OE1 204 12.38 0 -18.896 12.46 0 2A7R GMP REDUCTASE 2 SH HOMO SAPIENS OXIDOREDUCTASE 1.7.1.7
2BZN A 222 LKGHIISDGGCSCPGDVAKAF 7.6 224 30.51 9.5 LYS NZ  230 13.94 5.1 ASP OD2 227 4.4 0 -17.286 12.67 0 2A7R GMP REDUCTASE 2 SH HOMO SAPIENS OXIDOREDUCTASE 1.7.1.7
2BZN A 224 GHIISDGGCSCPGDVAKAFGA 7.6 222 0.34 6.2 LYS NZ  230 13.94 3.7 ASP OD2 227 4.4 31 -13.206 8.96 0 2A7R GMP REDUCTASE 2 SH HOMO SAPIENS OXIDOREDUCTASE 1.7.1.7
2BZN A 316 RDILGGIRSTCTYVGAAKLKE 14.5 222 0.34 9.6 ARG NH2 27 11.34 8.2 GLU OE1 326 2 0 -25.659 10.93 0 2A7R GMP REDUCTASE 2 SH HOMO SAPIENS OXIDOREDUCTASE 1.7.1.7
2C3C A 82 VDRWPFLGGSCPHNACVPHHL 3.4 87 19.5 5.5 ARG NH2 365 36.73 10.1 ASP OD2 353 21.8 18 -28.804 10.67 1 2C3D 2-OXOPROPYL-COM REDUCTASE SS XANTOBACTER AUTOTROPHICUS OXIDOREDUCTASE 1.8.1.5
2C3C A 87 FLGGSCPHNACVPHHLFSDCA 3.4 82 17.46 6.1 HIS NE2 91 10.38 7.2 GLU OE1 360 25.37 20 -20.445 14.03 1 2C3D 2-OXOPROPYL-COM REDUCTASE SS XANTOBACTER AUTOTROPHICUS OXIDOREDUCTASE 1.8.1.5
2C3C A 96 ACVPHHLFSDCAAELMLARTF 13.1 231 0 11.1 ARG NH2 104 0 7 ASP OD2 95 40.74 24 -27.401 12.18 0 2C3D 2-OXOPROPYL-COM REDUCTASE SH XANTOBACTER AUTOTROPHICUS OXIDOREDUCTASE 1.8.1.5
2C3C A 156 EQLNLEYILNCPAKVIDNHTV 22.9 82 17.46 5.6 LYS NZ  2 10.26 7.6 GLU OE2 167 28.11 14 -16.603 7.12 0 2C3D 2-OXOPROPYL-COM REDUCTASE SH XANTOBACTER AUTOTROPHICUS OXIDOREDUCTASE 1.8.1.5
2C3C A 231 GGSKTAVEYGCFFNATGRRTV 13.1 96 23.58 3.9 HIS NE2 394 0 9.1 GLU OE1 228 2.86 0 -39.999 8.6 0 2C3D 2-OXOPROPYL-COM REDUCTASE SH XANTOBACTER AUTOTROPHICUS OXIDOREDUCTASE 1.8.1.5
2COJ A 221 VRAWKGGTGDCKMGGNYGSSL 19.3 293 0 5 ARG NH1 126 14.36 3.5 ASP OD1 220 1.36 13 -17.82 12.12 0 2COI BRANCHED CHAIN AMINOTRANSFERASE SH HOMO SAPIENS TRANSFERASE 2.6.1.42
2COJ A 335 VREMFGSGTACVVCPVSDILY 4.8 338 4.02 7.8 LYS NZ 99 7.54 11.8 GLU OE1 257 6.12 4 -15.811 7.25 1 2COI BRANCHED CHAIN AMINOTRANSFERASE SS HOMO SAPIENS TRANSFERASE 2.6.1.42
2COJ A 338 MFGSGTACVVCPVSDILYKGE 4.8 335 3.64 12.3 LYS NZ 99 7.54 11.7 GLU OE1 327 0 4 -28.618 15.76 1 2COI BRANCHED CHAIN AMINOTRANSFERASE SS HOMO SAPIENS TRANSFERASE 2.6.1.42
2CRK A 146 SIKGYTLPPHCSRGERRAVEK 16.1 283 25.51 3.8 ARG NH1 151 0.22 5.6 GLU OE1 150 8.14 2 -13.853 6.57 0 Hurne, A.M., Chai, C.L., and Waring, P. 2000. Inactivation of rabbit muscle creatine kinase by reversible formation of an internal disulfide bond induced by the fungal toxin gliotoxin. J Biol Chem. 275: 25202-25206. PMID: 10827185. 10827185 Creatin Kinase Fungal Toxin Gliotoxin SH ORYCTOLAGUS CUNICULUS TRANSFERASE 2.7.3.2
2CRK A 283 WNEHLGYVLTCPSNLGTGLRG 7 74 0 8 ARG NH2 96 32.55 6.4 GLU OE1 232 16.46 26 -19.622 7.63 1 Hurne, A.M., Chai, C.L., and Waring, P. 2000. Inactivation of rabbit muscle creatine kinase by reversible formation of an internal disulfide bond induced by the fungal toxin gliotoxin. J Biol Chem. 275: 25202-25206. PMID: 10827185. 10827185 Creatin Kinase Fungal Toxin Gliotoxin intermol SS, SSG, SOOH ORYCTOLAGUS CUNICULUS TRANSFERASE 2.7.3.2
2CVX A 218 AGTPKPQMSSCFLVAMKEDSI 6 443 0 10.2 ARG NH2 293 16.33 4.3 GLU OE1 430 3.26 5 -17.087 14.12 1 1ZZD  RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE  SS SACCAROMYCES CEREVICIAE OXIDOREDUCTASE 1.17.4.1
2CVX A 429 LGVIKSSNLCCEIVEYSAPDE 7.1 428 27.55 11 ARG NH2 744 36.03 6.5 GLU OE2 430 0 0 -21.247 11.63 0 1ZZD  RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE  SH SACCAROMYCES CEREVICIAE OXIDOREDUCTASE 1.17.4.1
2CVX A 443 EYSAPDETAVCNLASVALPAF 6 218 5.41 11.5 ARG NH1 503 1.45 3.1 GLU OE2 433 0 0 -57.355 15.07 1 1ZZD  RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE  SS SACCAROMYCES CEREVICIAE OXIDOREDUCTASE 1.17.4.1
2CVX A 620 STSQILGYNECFEPVTSNMYS 10.1 428 27.55 8.1 ARG NH1 702 2.33 3.9 GLU OE2 622 3.19 2 -19.128 11.33 0 1ZZD  RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE  SH SACCAROMYCES CEREVICIAE OXIDOREDUCTASE 1.17.4.1
2CWT A 315 GQYANSLELGCDCLGDITYLS 8.9 317 5.02 12.6 ARG NH2 339 46.75 4.7 ASP OD1 316 32.84 61 -24.228 10.86 0 2CWU PHENYLETHYLAMINE OXIDASE  SH ARTHROBACTER GLOBIFORMIS OXIDOREDUCTASE 1.4.3.6
2CWT A 317 YANSLELGCDCLGDITYLSPV 3.1 343 0.5 7 HIS NE2 345 8.49 6.2 ASP OD2 316 6.77 5 -34.626 99.99 1 2CWU PHENYLETHYLAMINE OXIDASE  SS ARTHROBACTER GLOBIFORMIS OXIDOREDUCTASE 1.4.3.6
2CWT A 343 GNPREIRNGICMHEEDWGILA 3.1 317 5.02 5.4 HIS NE2 345 8.49 9.2 ASP OD2 316 6.77 1 -31.346 7.92 1 2CWU PHENYLETHYLAMINE OXIDASE  SS ARTHROBACTER GLOBIFORMIS OXIDOREDUCTASE 1.4.3.6
2CX4 A 49 IFFPAAFSPVCTKELCTFRDK 10.3 80 26.96 3.5 ARG NH1 122 0 5.4 GLU OE1 52 0 0 -5.17 5.26 1 2CX3 BACTERIOFERRITIN COMIGRATORY PROTEIN SS AEROPYRUM PERNIX K1 OXIDOREDUCTASE 1.11.1.15
2CX4 A 54 AFSPVCTKELCTFRDKAQLEK 10.6 49 0 3.9 ARG NH1 57 12.29 5.4 ASP OD2 58 13.17 13 -17.867 8.64 1 2CX3 BACTERIOFERRITIN COMIGRATORY PROTEIN SS AEROPYRUM PERNIX K1 OXIDOREDUCTASE 1.11.1.15
2CX4 A 80 VLAISVDSPWCLKKFKDENRL 10.3 49 0 10.3 LYS NZ  83 46.03 4.9 ASP OD1 76 21.81 27 -26.698 99.99 0 2CX3 BACTERIOFERRITIN COMIGRATORY PROTEIN SH AEROPYRUM PERNIX K1 OXIDOREDUCTASE 1.11.1.15
2FHK A 58 IMCPAEAGIDCGYVPPEETPD 20.6 96 19.75 3.7 ARG NH1 22 2.07 3.9 ASP OD2 57 0.1 20 -18.011 10.92 1 2FHJ TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE  SOH METHANOPYRUS KANDLERI TRANSFERASE 2.3.1.101
2FHK A 228 FLPASTNDAYCPTVEDNELPE 10.7 242 9.79 7.9 LYS NZ 210 5.09 6.5 ASP OD1 225 2.89 23 -26.271 9.46 0 2FHJ TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE  SH METHANOPYRUS KANDLERI TRANSFERASE 2.3.1.101
2FHK A 242 EDNELPEGVKCVYEIVINGLN 10.7 228 23.1 11.2 LYS NZ 241 42.68 10.9 GLU OE2 174 33.83 10 -36.767 12.6 0 2FHJ TETRAHYDROMETHANOPTERIN FORMYLTRANSFERASE  SH METHANOPYRUS KANDLERI TRANSFERASE 2.3.1.101
2FIV A 84 EIRDENYKTQCIFGNVCVLED 21.5 90 0 2.9 HIS NE2 72 1.57 5.7 GLU OE1 74 23.66 23 -15.02 7.54 1 3FIV FELINE IMMUNODEFICIENCY VIRUS PROTEASE SOOH FELINE IMMUNODEFICIENCY VIRUS HYDROLASE 3.4.23.16
2FIV A 90 YKTQCIFGNVCVLEDNSLIQP 21.5 84 23.21 7.4 ARG NH1 53 8.23 8.2 GLU OE2 93 2.17 0 -18.091 9.89 0 3FIV FELINE IMMUNODEFICIENCY VIRUS PROTEASE SH FELINE IMMUNODEFICIENCY VIRUS HYDROLASE 3.4.23.16
2FWF A 461 PVMLDLYADWCVACKEFEKYT 3.6 464 1.63 9.8 LYS NZ  465 24.58 7.7 GLU OE1 466 11.21 10 -44.967 4.91 1 2FWE THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD SS E-COLI OXIDOREDUCTASE 1.8.1.8
2FWF A 464 LDLYADWCVACKEFEKYTFSD 3.6 461 9.8 8.2 LYS NZ  465 24.58 5.7 ASP OD2 455 3.01 2 -20.789 9.71 1 2FWE THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD SS E-COLI OXIDOREDUCTASE 1.8.1.8
2GT3 A 51 GMEIAIFAMGCFWGVERLFWQ 8.6 198 46.81 9.7 HIS NE2 186 0.52 5.6 ASP OD1 129 30.08 17.5 -28.512 9.92 1 Boschi-Muller, S., Azza, S., Sanglier-Cianferani, S., Talfournier, F., Van Dorsselear, A., and Branlant, G. 2000. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. J Biol Chem. 275: 35908-35913. PMID: 10964927. 10964927 METHIONINE SULFOXIDE REDUCTASE A SS, SOH ESCHERICHIA COLI                                 OXIDOREDUCTASE 1.8.4.6                                                          
2GT3 A 86 YTPNPTYREVCSGDTGHAEAV 10.4 51 17.47 8.5 HIS NE2 186 0.52 6.8 ASP OD2 129 21.08 46.3 -18.757 8.79 0 Boschi-Muller, S., Azza, S., Sanglier-Cianferani, S., Talfournier, F., Van Dorsselear, A., and Branlant, G. 2000. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. J Biol Chem. 275: 35908-35913. PMID: 10964927. 10964927 METHIONINE SULFOXIDE REDUCTASE A SH ESCHERICHIA COLI                                 OXIDOREDUCTASE 1.8.4.6                                                          
2GT3 A 198 QYLHKNPYGYCGIGGIGVCLP 8.6 51 17.47 7.2 ARG NH1 57 33.19 11 GLU OE2 56 0.15 46.8 -12.71 9 1 Boschi-Muller, S., Azza, S., Sanglier-Cianferani, S., Talfournier, F., Van Dorsselear, A., and Branlant, G. 2000. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. J Biol Chem. 275: 35908-35913. PMID: 10964927. 10964927 METHIONINE SULFOXIDE REDUCTASE A SS ESCHERICHIA COLI                                 OXIDOREDUCTASE 1.8.4.6                                                          
2GT3 A 206 GYCGIGGIGVCLPPEA----- 25.4 198 46.81 10.6 ARG NH1 155 28.14 9 ASP OD1 164 29.51 55.3 -19.097 8.89 1 Boschi-Muller, S., Azza, S., Sanglier-Cianferani, S., Talfournier, F., Van Dorsselear, A., and Branlant, G. 2000. A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli. J Biol Chem. 275: 35908-35913. PMID: 10964927. 10964927 METHIONINE SULFOXIDE REDUCTASE A SS ESCHERICHIA COLI                                 OXIDOREDUCTASE 1.8.4.6                                                          
2HZE A 23 NKVTIFVKYTCPFCRNALDIL 5.7 26 0 7.4 LYS NZ  20 27.36 9.9 GLU OE1 54 17.94 55 -9.748 8.33 1 2HZF GLUTAREDOXIN-1  SS ECTROMELIA VIRUS OXIDOREDUCTASE 1.8.5.1
2HZE A 26 TIFVKYTCPFCRNALDILNKF 5.7 23 55.11 8.7 LYS NZ  20 27.36 8.5 ASP OD1 47 1.53 0 -10.993 6.97 1 2HZF GLUTAREDOXIN-1  SS ECTROMELIA VIRUS OXIDOREDUCTASE 1.8.5.1
2IDV A 113 KIEPKWEDPICANGGKWTISC 3.7 151 0 5 HIS NE2 199 0 4.8 ASP OD2 110 0 0 -17.739 12.34 1 2IDR EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-1 SS TRITICUM AESTIVUM TRANSLATION REGULATOR                    N/A
2IDV A 123 CANGGKWTISCGRGKSDTFWL 17.9 99 0 9.1 ARG NH1 125 3.72 4.8 GLU OE2 162 0 0.2 -28.546 8.45 0 2IDR EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-4 SH TRITICUM AESTIVUM TRANSLATION REGULATOR                    N/A
2IDV A 151 GEQFDFGDEICGAVVSVRQKQ 3.7 113 0 4.7 LYS NZ  169 6.77 7.1 GLU OE2 149 0 0 -27.639 8.63 1 2IDR EUKARYOTIC TRANSLATION INITIATION FACTOR 4E-2 SS TRITICUM AESTIVUM TRANSLATION REGULATOR                    N/A
2IZZ A 95 DIEDRHIVVSCAAGVTISSIE 4 120 0 10.9 ARG NH2 119 0.28 12.6 GLU OE2 164 0 0 -30.462 14.8 1 2GER PYRROLINE-5-CARBOXYLATE REDUCTASE 1 SS HOMO SAPIENS OXIDOREDUCTASE 1.5.1.2
2IZZ A 120 AFRPAPRVIRCMTNTPVVVRE 4 95 0.01 10.1 ARG NH2 119 0.28 11.5 GLU OE2 150 10.93 0 -17.087 12.12 1 2GER PYRROLINE-5-CARBOXYLATE REDUCTASE 1 SS HOMO SAPIENS OXIDOREDUCTASE 1.5.1.2
2IZZ A 159 MEQLLSSVGFCTEVEEDLIDA 7.5 120 0 12.6 ARG NH2 129 33.45 5.1 GLU OE2 150 10.93 0 -22.299 10.13 0 2GER PYRROLINE-5-CARBOXYLATE REDUCTASE 1 SH HOMO SAPIENS OXIDOREDUCTASE 1.5.1.2
2IZZ A 262 SLLINAVEASCIRTRELQSM- 16.5 120 0 3.6 ARG NH2 266 27.28 5.8 ASP OD2 168 22.1 7 -25.044 8.08 0 2GER PYRROLINE-5-CARBOXYLATE REDUCTASE 1 SH HOMO SAPIENS OXIDOREDUCTASE 1.5.1.2
2OA0 A 12 EAAHSKSTEECLAYFGVSETT 31.9 420 0 5.7 ARG NH1 164 0 6.8 GLU OE1 11 5.36 0.9 -24.542 8.38 0 Cohen, R.A. and Adachi, T. 2006. Nitric-oxide-induced vasodilatation: regulation by physiologic s-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase. Trends Cardiovasc Med. 16: 109-114. PMID: 16713532. 16713532 SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 1                  SH ORYCTOLAGUS CUNICULUS HYDROLASE 3.6.3.8                                                          
2OA0 A 70 LLVRILLLAACISFVLAWFEE 14.3 268 9.47 10.4 ARG NH1 63 49.59 14.6 GLU OE1 90 26.78 42.8 -15.982 8.95 0 Cohen, R.A. and Adachi, T. 2006. Nitric-oxide-induced vasodilatation: regulation by physiologic s-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase. Trends Cardiovasc Med. 16: 109-114. PMID: 16713532. 16713532 SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 2 SH ORYCTOLAGUS CUNICULUS HYDROLASE 3.6.3.8                                                          
2OA0 A 268 EQLSKVISLICVAVWLINHGG 14.3 70 42.79 12.9 LYS NZ  262 49.07 13.5 GLU OE2 309 0 9.5 -16.279 9.78 0 Cohen, R.A. and Adachi, T. 2006. Nitric-oxide-induced vasodilatation: regulation by physiologic s-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase. Trends Cardiovasc Med. 16: 109-114. PMID: 16713532. 16713532 SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 3 SH ORYCTOLAGUS CUNICULUS HYDROLASE 3.6.3.8                                                          
2OA0 A 417 FDGLVELATICALCNDSSLDF 8.7 420 0 7.5 LYS NZ  515 0.21 10 GLU OE2 442 7.27 0 -17.624 12.46 0 Cohen, R.A. and Adachi, T. 2006. Nitric-oxide-induced vasodilatation: regulation by physiologic s-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase. Trends Cardiovasc Med. 16: 109-114. PMID: 16713532. 16713532 SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 9 SH ORYCTOLAGUS CUNICULUS HYDROLASE 3.6.3.8                                                          
2OA0 A 498 SRDRKSMSVYCSPAKSSRAAV 8.1 420 0 6.8 LYS NZ  481 6.92 8.8 GLU OE1 482 20.91 0 -18.534 10.13 0 Cohen, R.A. and Adachi, T. 2006. Nitric-oxide-induced vasodilatation: regulation by physiologic s-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase. Trends Cardiovasc Med. 16: 109-114. PMID: 16713532. 16713532 SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 12 SH ORYCTOLAGUS CUNICULUS HYDROLASE 3.6.3.8                                                          
2OA0 A 674 AEQREACRRACCFARVEPSHK 7.6 636 0 4.1 ARG NH1 651 30.99 8.1 GLU OE1 646 9.06 10.1 -17.889 7.61 1 Cohen, R.A. and Adachi, T. 2006. Nitric-oxide-induced vasodilatation: regulation by physiologic s-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase. Trends Cardiovasc Med. 16: 109-114. PMID: 16713532. 16713532 SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 18 SSG ORYCTOLAGUS CUNICULUS HYDROLASE 3.6.3.8                                                          
2OA0 A 774 LISSNVGEVVCIFLTAALGLP 14.9 268 9.47 13.5 HIS NE2 944 0 8.6 GLU OE1 771 0 0 -27.722 9.65 0 Cohen, R.A. and Adachi, T. 2006. Nitric-oxide-induced vasodilatation: regulation by physiologic s-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase. Trends Cardiovasc Med. 16: 109-114. PMID: 16713532. 16713532 SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 20 SH ORYCTOLAGUS CUNICULUS HYDROLASE 3.6.3.8                                                          
2OA0 A 876 TYHQLTHFMQCTEDHPHEIFE 23.4 774 0 8.2 HIS NE2 882 31.43 4.6 ASP OD1 879 3.52 42.1 -13.321 9 0 Cohen, R.A. and Adachi, T. 2006. Nitric-oxide-induced vasodilatation: regulation by physiologic s-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase. Trends Cardiovasc Med. 16: 109-114. PMID: 16713532. 16713532 SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 21 SH ORYCTOLAGUS CUNICULUS HYDROLASE 3.6.3.8                                                          
2OA0 A 910 ALSVLVTIEMCNALNSLSENQ 13 938 61.39 11.8 LYS NZ  985 1.2 9.2 GLU OE2 908 0 15.4 -28.192 10.5 0 Cohen, R.A. and Adachi, T. 2006. Nitric-oxide-induced vasodilatation: regulation by physiologic s-glutathiolation and pathologic oxidation of the sarcoplasmic endoplasmic reticulum calcium ATPase. Trends Cardiovasc Med. 16: 109-114. PMID: 16713532. 16713532 SARCOPLASMIC/ENDOPLASMIC RETICULUM CALCIUM ATPASE 22 SH ORYCTOLAGUS CUNICULUS HYDROLASE 3.6.3.8                                                          
3PGT A 14 TVVYFPVRGRCAALRMLLADQ 11.8 47 0 4.8 ARG NH2 18 8.17 6.2 GLU OE1 30 1.92 0 -16.365 10.44 0 4PGT GLUTATHIONE S-TRANSFERASE SH HOMO SAPIENS TRANSFERASE 2.5.1.18
3PGT A 47 TWQEGSLKASCLYGQLPKFQD 11.8 14 0.2 5.8 LYS NZ 54 28.58 10.1 GLU OE1 31 16.95 0 -31.191 8.65 0 4PGT GLUTATHIONE S-TRANSFERASE SH HOMO SAPIENS TRANSFERASE 2.5.1.18
3PGT A 101 MVNDGVEDLRCKYISLIYTNY 15.1 14 0.2 3.9 ARG NH2 13 9.46 3.3 GLU OE2 97 12.93 37 -27.959 12.74 1 4PGT GLUTATHIONE S-TRANSFERASE SOH HOMO SAPIENS TRANSFERASE 2.5.1.18
17283067
17283067
17521670
17521670
17521670
17521670
17521670
17521670
10827185
10827185
10827185
10827185
10964927
10964927
10964927
10964927
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532
16713532