eF-site ID 1qin-AB PDB Code 1qin Chain A, B click to enlarge Title HUMAN GLYOXALASE I COMPLEXED WITH S-(N-HYDROXY-N-P-IODOPHENYLCARBAMOYL) GLUTATHIONE Classification LYASE Compound PROTEIN (LACTOYLGLUTATHIONE LYASE) Source Homo sapiens (Human) (LGUL_HUMAN) Sequence A:  GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDF YTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEK IAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHI GIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPD GYWIEILNPNKMATLM B:  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 A residue 60 type sequence C description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 10) chain A residue 62 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 11) chain A residue 65 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 12) chain A residue 67 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 13) chain A residue 69 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 14) chain A residue 71 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 15) chain A residue 88 type sequence I description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 16) chain A residue 92 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 17) chain B residue 157 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 18) chain B residue 160 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 19) chain B residue 162 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 20) chain B residue 174 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 21) chain B residue 179 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 22) chain B residue 183 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 23) chain B residue 60 type sequence C description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 24) chain B residue 62 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 25) chain B residue 65 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 26) chain B residue 67 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 27) chain B residue 69 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 28) chain B residue 71 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 29) chain B residue 88 type sequence I description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 30) chain B residue 92 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 31) chain A residue 157 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 32) chain A residue 160 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 33) chain A residue 162 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 34) chain A residue 174 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 35) chain A residue 179 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 36) chain A residue 183 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 37) 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 38) 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 39) 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 40) 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 41) 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 42) 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 43) chain A residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN B 301 source : AC1 44) chain A residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN B 301 source : AC1 45) chain B residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN B 301 source : AC1 46) chain B residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN B 301 source : AC1 47) chain A residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 48) chain A residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 49) chain B residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 50) chain B residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 51) chain A residue 122 type sequence R description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 52) chain A residue 126 type sequence H description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 53) chain A residue 150 type sequence K description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 54) chain A residue 155 type sequence G description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 55) chain A residue 156 type sequence K description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 56) chain A residue 157 type sequence M description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 57) chain A residue 160 type sequence L description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 58) chain A residue 162 type sequence F description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 59) chain A residue 172 type sequence E description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 60) chain A residue 179 type sequence M description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 61) chain A residue 183 type sequence M description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 62) chain B residue 33 type sequence Q description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 63) chain B residue 37 type sequence R description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 64) chain B residue 67 type sequence F description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 65) chain B residue 69 type sequence L description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 66) chain B residue 71 type sequence F description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 67) chain B residue 99 type sequence E description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 68) chain B residue 101 type sequence T description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 69) chain B residue 103 type sequence N description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 70) chain A residue 33 type sequence Q description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 71) chain A residue 37 type sequence R description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 72) chain A residue 67 type sequence F description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 73) chain A residue 69 type sequence L description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 74) chain A residue 71 type sequence F description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 75) chain A residue 99 type sequence E description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 76) chain A residue 101 type sequence T description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 77) chain A residue 103 type sequence N description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 78) chain B residue 122 type sequence R description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 79) chain B residue 126 type sequence H description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 80) chain B residue 150 type sequence K description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 81) chain B residue 155 type sequence G description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 82) chain B residue 156 type sequence K description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 83) chain B residue 157 type sequence M description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 84) chain B residue 160 type sequence L description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 85) chain B residue 162 type sequence F description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 86) chain B residue 172 type sequence E description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 87) chain B residue 179 type sequence M description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 88) chain A residue 34 type catalytic sequence T description 32 source MCSA : MCSA1 89) chain A residue 100 type catalytic sequence L description 32 source MCSA : MCSA1 90) chain A residue 127 type catalytic sequence I description 32 source MCSA : MCSA1 91) chain A residue 173 type catalytic sequence I description 32 source MCSA : MCSA1 92) chain B residue 34 type catalytic sequence T description 32 source MCSA : MCSA2 93) chain B residue 100 type catalytic sequence L description 32 source MCSA : MCSA2 94) chain B residue 127 type catalytic sequence I description 32 source MCSA : MCSA2 95) chain B residue 173 type catalytic sequence I description 32 source MCSA : MCSA2 96) 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 97) 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 98) 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 99) 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 100) 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 101) 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 102) chain A residue 38 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 103) chain A residue 104 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 104) chain B residue 38 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 105) chain B residue 104 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 106) chain A residue 123 type BINDING sequence G description in other chain source Swiss-Prot : SWS_FT_FI4 107) chain A residue 157 type BINDING sequence M description in other chain source Swiss-Prot : SWS_FT_FI4 108) chain B residue 123 type BINDING sequence G description in other chain source Swiss-Prot : SWS_FT_FI4 109) chain B residue 157 type BINDING sequence M description in other chain source Swiss-Prot : SWS_FT_FI4 110) chain A residue 33-54 type prosite sequence QTMLRVKDPKKSLDFYTRVLGM description GLYOXALASE_I_1 Glyoxalase I signature 1. QTmLrVkdpkKSldFYtrvLGM source prosite : PS00934 111) chain A residue 117-133 type prosite sequence GNSDPRGFGHIGIAVPD description GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD source prosite : PS00935 112) chain A residue 148 type MOD_RES sequence F description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 113) chain B residue 148 type MOD_RES sequence F description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 114) 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 115) 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 116) 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 117) 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 118) chain A residue 88 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 119) chain B residue 88 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 120) chain A residue 107 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 121) chain B residue 107 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 122) chain A residue 139 type MOD_RES sequence K description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 123) chain B residue 139 type MOD_RES sequence K description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9

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