eF-site ID 1fro-ABCD PDB Code 1fro Chain A, B, C, D click to enlarge Title HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR Classification LACTOYLGLUTATHIONE LYASE Compound LACTOYLGLUTATHIONE LYASE Source null (LGUL_HUMAN) Sequence A:  GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDF YTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEK IAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHI GIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPD GYWIEILNPNKMATLM B:  GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDF YTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEK IAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHI GIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPD GYWIEILNPNKMATLM C:  GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDF YTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEK IAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHI GIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPD GYWIEILNPNKMATLM D:  GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDF YTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEK IAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHI GIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPD GYWIEILNPNKMATLM 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 A 201 source : AC1 86) chain A residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 87) chain B residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 88) chain B residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 89) chain A residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN B 201 source : AC2 90) chain A residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN B 201 source : AC2 91) chain B residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN B 201 source : AC2 92) chain B residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN B 201 source : AC2 93) chain C residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN C 201 source : AC3 94) chain C residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN C 201 source : AC3 95) chain D residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN C 201 source : AC3 96) chain D residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN C 201 source : AC3 97) chain C residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN D 201 source : AC4 98) chain C residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN D 201 source : AC4 99) chain D residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN D 201 source : AC4 100) chain D residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN D 201 source : AC4 101) chain A residue 122 type sequence R description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 102) chain A residue 150 type sequence K description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 103) chain A residue 157 type sequence M description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 104) chain A residue 162 type sequence F description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 105) chain A residue 172 type sequence E description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 106) chain A residue 183 type sequence M description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 107) chain B residue 37 type sequence R description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 108) chain B residue 62 type sequence F description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 109) chain B residue 67 type sequence F description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 110) chain B residue 101 type sequence T description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 111) chain B residue 103 type sequence N description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 112) chain C residue 17 type sequence S description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 113) chain A residue 37 type sequence R description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 114) chain A residue 62 type sequence F description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 115) chain A residue 67 type sequence F description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 116) chain A residue 101 type sequence T description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 117) chain A residue 103 type sequence N description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 118) chain B residue 122 type sequence R description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 119) chain B residue 150 type sequence K description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 120) chain B residue 157 type sequence M description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 121) chain B residue 162 type sequence F description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 122) chain B residue 172 type sequence E description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 123) chain B residue 183 type sequence M description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 124) chain D residue 154 type sequence D description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 125) chain D residue 158 type sequence K description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 126) chain C residue 122 type sequence R description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 127) chain C residue 150 type sequence K description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 128) chain C residue 157 type sequence M description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 129) chain C residue 162 type sequence F description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 130) chain C residue 172 type sequence E description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 131) chain C residue 183 type sequence M description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 132) chain D residue 37 type sequence R description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 133) chain D residue 62 type sequence F description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 134) chain D residue 67 type sequence F description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 135) chain D residue 101 type sequence T description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 136) chain D residue 103 type sequence N description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 137) chain C residue 37 type sequence R description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 138) chain C residue 62 type sequence F description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 139) chain C residue 67 type sequence F description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 140) chain C residue 101 type sequence T description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 141) chain C residue 103 type sequence N description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 142) chain D residue 122 type sequence R description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 143) chain D residue 150 type sequence K description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 144) chain D residue 157 type sequence M description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 145) chain D residue 162 type sequence F description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 146) chain D residue 172 type sequence E description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 147) chain D residue 183 type sequence M description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 148) chain A residue 33 type catalytic sequence Q description 32 source MCSA : MCSA1 149) chain A residue 99 type catalytic sequence E description 32 source MCSA : MCSA1 150) chain A residue 126 type catalytic sequence H description 32 source MCSA : MCSA1 151) chain A residue 172 type catalytic sequence E description 32 source MCSA : MCSA1 152) chain B residue 33 type catalytic sequence Q description 32 source MCSA : MCSA2 153) chain B residue 99 type catalytic sequence E description 32 source MCSA : MCSA2 154) chain B residue 126 type catalytic sequence H description 32 source MCSA : MCSA2 155) chain B residue 172 type catalytic sequence E description 32 source MCSA : MCSA2 156) chain C residue 33 type catalytic sequence Q description 32 source MCSA : MCSA3 157) chain C residue 99 type catalytic sequence E description 32 source MCSA : MCSA3 158) chain C residue 126 type catalytic sequence H description 32 source MCSA : MCSA3 159) chain C residue 172 type catalytic sequence E description 32 source MCSA : MCSA3 160) chain D residue 33 type catalytic sequence Q description 32 source MCSA : MCSA4 161) chain D residue 99 type catalytic sequence E description 32 source MCSA : MCSA4 162) chain D residue 126 type catalytic sequence H description 32 source MCSA : MCSA4 163) chain D residue 172 type catalytic sequence E description 32 source MCSA : MCSA4 164) chain A residue 172 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI1 165) chain B residue 172 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI1 166) chain C residue 172 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI1 167) chain D residue 172 type ACT_SITE sequence E description Proton donor/acceptor => ECO:0000269|PubMed:10521255, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI1 168) chain C residue 33 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 169) chain C residue 99 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 170) chain D residue 33 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 171) chain D residue 99 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 172) chain A residue 33 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 173) chain A residue 99 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 174) chain B residue 33 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 175) chain B residue 99 type BINDING sequence E description BINDING => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI2 176) chain C residue 37 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 177) chain C residue 103 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 178) chain D residue 37 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 179) chain D residue 103 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 180) chain A residue 37 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 181) chain A residue 103 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 182) chain B residue 37 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 183) chain B residue 103 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 184) chain C residue 122 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI4 185) chain C residue 156 type BINDING sequence K description in other chain source Swiss-Prot : SWS_FT_FI4 186) chain D residue 122 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI4 187) chain D residue 156 type BINDING sequence K description in other chain source Swiss-Prot : SWS_FT_FI4 188) chain A residue 122 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI4 189) chain A residue 156 type BINDING sequence K description in other chain source Swiss-Prot : SWS_FT_FI4 190) chain B residue 122 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI4 191) chain B residue 156 type BINDING sequence K description in other chain source Swiss-Prot : SWS_FT_FI4 192) chain A residue 87 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 193) chain B residue 87 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 194) chain C residue 87 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 195) chain D residue 87 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 196) chain A residue 147 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 197) chain B residue 147 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 198) chain C residue 147 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 199) chain D residue 147 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 200) chain A residue 33-54 type prosite sequence QTMLRVKDPKKSLDFYTRVLGM description GLYOXALASE_I_1 Glyoxalase I signature 1. QTmLrVkdpkKSldFYtrvLGM source prosite : PS00934 201) chain A residue 117-133 type prosite sequence GNSDPRGFGHIGIAVPD description GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD source prosite : PS00935 202) chain A residue 126 type BINDING sequence H description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 203) chain A residue 172 type BINDING sequence E description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 204) chain B residue 126 type BINDING sequence H description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 205) chain B residue 172 type BINDING sequence E description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 206) chain C residue 126 type BINDING sequence H description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 207) chain C residue 172 type BINDING sequence E description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 208) chain D residue 126 type BINDING sequence H description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 209) chain D residue 172 type BINDING sequence E description in other chain => ECO:0000269|PubMed:23122816, ECO:0000269|PubMed:9218781, ECO:0000269|PubMed:9705294 source Swiss-Prot : SWS_FT_FI5 210) chain A residue 106 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 211) chain B residue 106 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 212) chain C residue 106 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 213) chain D residue 106 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 214) chain A residue 138 type MOD_RES sequence C description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 215) chain B residue 138 type MOD_RES sequence C description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 216) chain C residue 138 type MOD_RES sequence C description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 217) chain D residue 138 type MOD_RES sequence C description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9

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