eF-site ID 1qip-ABCD PDB Code 1qip Chain A, B, C, D click to enlarge Title HUMAN GLYOXALASE I COMPLEXED WITH S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE Classification LYASE Compound PROTEIN (LACTOYLGLUTATHIONE LYASE) Source null (LGUL_HUMAN) Sequence A:  GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDF YTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEK IAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHI GIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPD GYWIEILNPNKMATLM B:  AEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKD PKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDI PKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSD PRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGL AFIQDPDGYWIEILNPNKMATLM C:  GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDF YTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEK IAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHI GIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPD GYWIEILNPNKMATLM D:  AEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKD PKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDI PKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSD PRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGL AFIQDPDGYWIEILNPNKMATLM Description Functional site 1) chain A residue 33 type sequence Q description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN1 2) chain A residue 99 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN1 3) chain B residue 126 type sequence H description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN1 4) chain B residue 172 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN1 5) chain B residue 33 type sequence Q description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN2 6) chain B residue 99 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN2 7) chain A residue 126 type sequence H description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN2 8) chain A residue 172 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN2 9) chain C residue 33 type sequence Q description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN3 10) chain C residue 99 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN3 11) chain D residue 126 type sequence H description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN3 12) chain D residue 172 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN3 13) chain D residue 33 type sequence Q description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN4 14) chain D residue 99 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN4 15) chain C residue 126 type sequence H description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN4 16) chain C residue 172 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN4 17) chain A residue 60 type sequence C description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 18) chain A residue 62 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 19) chain A residue 65 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 20) chain A residue 67 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 21) chain A residue 69 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 22) chain A residue 71 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 23) chain A residue 88 type sequence I description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 24) chain A residue 92 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 25) chain B residue 157 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 26) chain B residue 160 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 27) chain B residue 162 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 28) chain B residue 174 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 29) chain B residue 179 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 30) chain B residue 183 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 31) chain B residue 60 type sequence C description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 32) chain B residue 62 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 33) chain B residue 65 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 34) chain B residue 67 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 35) chain B residue 69 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 36) chain B residue 71 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 37) chain B residue 88 type sequence I description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 38) chain B residue 92 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 39) chain A residue 157 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 40) chain A residue 160 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 41) chain A residue 162 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 42) chain A residue 174 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 43) chain A residue 179 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 44) chain A residue 183 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 45) chain C residue 60 type sequence C description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 46) chain C residue 62 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 47) chain C residue 65 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 48) chain C residue 67 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 49) chain C residue 69 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 50) chain C residue 71 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 51) chain C residue 88 type sequence I description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 52) chain C residue 92 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 53) chain D residue 157 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 54) chain D residue 160 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 55) chain D residue 162 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 56) chain D residue 174 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 57) chain D residue 179 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 58) chain D residue 183 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 59) chain D residue 60 type sequence C description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 60) chain D residue 62 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 61) chain D residue 65 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 62) chain D residue 67 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 63) chain D residue 69 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 64) chain D residue 71 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 65) chain D residue 88 type sequence I description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 66) chain D residue 92 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 67) chain C residue 157 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 68) chain C residue 160 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 69) chain C residue 162 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 70) chain C residue 174 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 71) chain C residue 179 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 72) chain C residue 183 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 73) chain B residue 37 type sequence R description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1. source : GH2 74) chain B residue 103 type sequence N description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1. source : GH2 75) chain A residue 122 type sequence R description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1. source : GH2 76) chain A residue 37 type sequence R description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2. source : GH1 77) chain A residue 103 type sequence N description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2. source : GH1 78) chain B residue 122 type sequence R description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2. source : GH1 79) chain D residue 37 type sequence R description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1. source : GH4 80) chain D residue 103 type sequence N description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1. source : GH4 81) chain C residue 122 type sequence R description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN1 HYD1 AND GSH1. source : GH4 82) chain C residue 37 type sequence R description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2. source : GH3 83) chain C residue 103 type sequence N description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2. source : GH3 84) chain D residue 122 type sequence R description BINDING SITE FOR GSH MOIETY - SUBSTRATE BINDING SITE IS FORMED BY ZN2 HYD2 AND GSH2. source : GH3 85) chain A residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN B 901 source : AC1 86) chain A residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN B 901 source : AC1 87) chain B residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN B 901 source : AC1 88) chain B residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN B 901 source : AC1 89) chain A residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN A 902 source : AC2 90) chain A residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN A 902 source : AC2 91) chain B residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN A 902 source : AC2 92) chain B residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN A 902 source : AC2 93) chain C residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN D 903 source : AC3 94) chain C residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN D 903 source : AC3 95) chain D residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN D 903 source : AC3 96) chain D residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN D 903 source : AC3 97) chain C residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN C 904 source : AC4 98) chain C residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN C 904 source : AC4 99) chain D residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN C 904 source : AC4 100) chain D residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN C 904 source : AC4 101) chain A residue 122 type sequence R description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 102) chain A residue 160 type sequence L description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 103) chain A residue 162 type sequence F description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 104) chain A residue 172 type sequence E description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 105) chain A residue 179 type sequence M description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 106) chain A residue 182 type sequence L description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 107) chain B residue 37 type sequence R description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 108) chain B residue 60 type sequence C description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 109) chain B residue 67 type sequence F description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 110) chain B residue 88 type sequence I description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 111) chain B residue 92 type sequence L description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 112) chain B residue 101 type sequence T description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 113) chain B residue 103 type sequence N description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 114) chain C residue 17 type sequence S description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 115) chain A residue 37 type sequence R description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 116) chain A residue 58 type sequence Q description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 117) chain A residue 60 type sequence C description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 118) chain A residue 67 type sequence F description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 119) chain A residue 71 type sequence F description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 120) chain A residue 88 type sequence I description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 121) chain A residue 92 type sequence L description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 122) chain A residue 101 type sequence T description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 123) chain A residue 103 type sequence N description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 124) chain B residue 122 type sequence R description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 125) chain B residue 157 type sequence M description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 126) chain B residue 160 type sequence L description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 127) chain B residue 162 type sequence F description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 128) chain B residue 170 type sequence W description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 129) chain D residue 154 type sequence D description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 130) chain D residue 158 type sequence K description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 131) chain A residue 17 type sequence S description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 132) chain C residue 122 type sequence R description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 133) chain C residue 157 type sequence M description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 134) chain C residue 160 type sequence L description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 135) chain C residue 162 type sequence F description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 136) chain C residue 179 type sequence M description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 137) chain D residue 37 type sequence R description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 138) chain D residue 60 type sequence C description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 139) chain D residue 67 type sequence F description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 140) chain D residue 88 type sequence I description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 141) chain D residue 92 type sequence L description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 142) chain D residue 101 type sequence T description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 143) chain D residue 103 type sequence N description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 144) chain C residue 37 type sequence R description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 145) chain C residue 60 type sequence C description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 146) chain C residue 67 type sequence F description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 147) chain C residue 88 type sequence I description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 148) chain C residue 92 type sequence L description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 149) chain C residue 101 type sequence T description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 150) chain C residue 103 type sequence N description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 151) chain D residue 122 type sequence R description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 152) chain D residue 157 type sequence M description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 153) chain D residue 160 type sequence L description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 154) chain D residue 162 type sequence F description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 155) chain D residue 179 type sequence M description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 156) chain A residue 58 type sequence Q description BINDING SITE FOR RESIDUE BME A 204 source : AC9 157) chain A residue 59 type sequence K description BINDING SITE FOR RESIDUE BME A 204 source : AC9 158) chain A residue 60 type sequence C description BINDING SITE FOR RESIDUE BME A 204 source : AC9 159) chain A residue 62 type sequence F description BINDING SITE FOR RESIDUE BME A 204 source : AC9 160) chain B residue 58 type sequence Q description BINDING SITE FOR RESIDUE BME B 204 source : BC1 161) chain B residue 59 type sequence K description BINDING SITE FOR RESIDUE BME B 204 source : BC1 162) chain B residue 60 type sequence C description BINDING SITE FOR RESIDUE BME B 204 source : BC1 163) chain B residue 84 type sequence K description BINDING SITE FOR RESIDUE BME B 204 source : BC1 164) chain C residue 58 type sequence Q description BINDING SITE FOR RESIDUE BME C 204 source : BC2 165) chain C residue 60 type sequence C description BINDING SITE FOR RESIDUE BME C 204 source : BC2 166) chain D residue 60 type sequence C description BINDING SITE FOR RESIDUE BME D 204 source : BC3 167) chain D residue 62 type sequence F description BINDING SITE FOR RESIDUE BME D 204 source : BC3 168) chain A residue 173 type ACT_SITE sequence I description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI1 169) chain B residue 173 type ACT_SITE sequence I description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI1 170) chain C residue 173 type ACT_SITE sequence I description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI1 171) chain D residue 173 type ACT_SITE sequence I description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI1 172) chain A residue 34 type BINDING sequence T description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 173) chain A residue 100 type BINDING sequence L description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 174) chain B residue 34 type BINDING sequence T description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 175) chain B residue 100 type BINDING sequence L description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 176) chain C residue 34 type BINDING sequence T description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 177) chain C residue 100 type BINDING sequence L description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 178) chain D residue 34 type BINDING sequence T description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 179) chain D residue 100 type BINDING sequence L description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 180) chain A residue 38 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 181) chain A residue 104 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 182) chain C residue 38 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 183) chain C residue 104 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 184) chain D residue 38 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 185) chain D residue 104 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 186) chain B residue 38 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 187) chain B residue 104 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 188) chain A residue 123 type BINDING sequence G description in other chain source Swiss-Prot : SWS_FT_FI4 189) chain A residue 157 type BINDING sequence M description in other chain source Swiss-Prot : SWS_FT_FI4 190) chain C residue 123 type BINDING sequence G description in other chain source Swiss-Prot : SWS_FT_FI4 191) chain C residue 157 type BINDING sequence M description in other chain source Swiss-Prot : SWS_FT_FI4 192) chain D residue 123 type BINDING sequence G description in other chain source Swiss-Prot : SWS_FT_FI4 193) chain D residue 157 type BINDING sequence M description in other chain source Swiss-Prot : SWS_FT_FI4 194) chain B residue 123 type BINDING sequence G description in other chain source Swiss-Prot : SWS_FT_FI4 195) chain B residue 157 type BINDING sequence M description in other chain source Swiss-Prot : SWS_FT_FI4 196) chain A residue 88 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 197) chain B residue 88 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 198) chain D residue 88 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 199) chain C residue 88 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 200) chain A residue 107 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 201) chain B residue 107 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 202) chain D residue 107 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 203) chain C residue 107 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 204) chain A residue 139 type MOD_RES sequence K description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 205) chain B residue 139 type MOD_RES sequence K description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 206) chain D residue 139 type MOD_RES sequence K description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 207) chain C residue 139 type MOD_RES sequence K description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 208) chain A residue 148 type MOD_RES sequence F description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 209) chain B residue 148 type MOD_RES sequence F description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 210) chain D residue 148 type MOD_RES sequence F description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 211) chain C residue 148 type MOD_RES sequence F description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 212) chain A residue 34 type catalytic sequence T description 32 source MCSA : MCSA1 213) chain A residue 100 type catalytic sequence L description 32 source MCSA : MCSA1 214) chain A residue 127 type catalytic sequence I description 32 source MCSA : MCSA1 215) chain A residue 173 type catalytic sequence I description 32 source MCSA : MCSA1 216) chain B residue 34 type catalytic sequence T description 32 source MCSA : MCSA2 217) chain B residue 100 type catalytic sequence L description 32 source MCSA : MCSA2 218) chain B residue 127 type catalytic sequence I description 32 source MCSA : MCSA2 219) chain B residue 173 type catalytic sequence I description 32 source MCSA : MCSA2 220) chain C residue 34 type catalytic sequence T description 32 source MCSA : MCSA3 221) chain C residue 100 type catalytic sequence L description 32 source MCSA : MCSA3 222) chain C residue 127 type catalytic sequence I description 32 source MCSA : MCSA3 223) chain C residue 173 type catalytic sequence I description 32 source MCSA : MCSA3 224) chain D residue 34 type catalytic sequence T description 32 source MCSA : MCSA4 225) chain D residue 100 type catalytic sequence L description 32 source MCSA : MCSA4 226) chain D residue 127 type catalytic sequence I description 32 source MCSA : MCSA4 227) chain D residue 173 type catalytic sequence I description 32 source MCSA : MCSA4 228) chain A residue 33-54 type prosite sequence QTMLRVKDPKKSLDFYTRVLGM description GLYOXALASE_I_1 Glyoxalase I signature 1. QTmLrVkdpkKSldFYtrvLGM source prosite : PS00934 229) chain A residue 117-133 type prosite sequence GNSDPRGFGHIGIAVPD description GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD source prosite : PS00935 230) chain A residue 127 type BINDING sequence I description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 231) chain A residue 173 type BINDING sequence I description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 232) chain B residue 127 type BINDING sequence I description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 233) chain B residue 173 type BINDING sequence I description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 234) chain C residue 127 type BINDING sequence I description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 235) chain C residue 173 type BINDING sequence I description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 236) chain D residue 127 type BINDING sequence I description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 237) chain D residue 173 type BINDING sequence I description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 238) chain B residue 2 type MOD_RES sequence E description N-acetylalanine => ECO:0000269|PubMed:20454679, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI6 239) chain D residue 2 type MOD_RES sequence E description N-acetylalanine => ECO:0000269|PubMed:20454679, ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712 source Swiss-Prot : SWS_FT_FI6

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