eF-site ID 1qip-D PDB Code 1qip Chain D click to enlarge Title HUMAN GLYOXALASE I COMPLEXED WITH S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE Classification LYASE Compound PROTEIN (LACTOYLGLUTATHIONE LYASE) Source null (LGUL_HUMAN) Sequence D:  AEPQPPSGGLTDEAALSCCSDADPSTKDFLLQQTMLRVKD PKKSLDFYTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDI PKEKDEKIAWALSRKATLELTHNWGTEDDETQSYHNGNSD PRGFGHIGIAVPDVYSACKRFEELGVKFVKKPDDGKMKGL AFIQDPDGYWIEILNPNKMATLM Description Functional site 1) chain D residue 126 type sequence H description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN3 2) chain D residue 172 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN3 3) chain D residue 33 type sequence Q description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN4 4) chain D residue 99 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN4 5) chain D residue 157 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 6) chain D residue 160 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 7) chain D residue 162 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 8) chain D residue 174 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 9) chain D residue 179 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 10) chain D residue 183 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 11) chain D residue 60 type sequence C description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 12) chain D residue 62 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 13) chain D residue 65 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 14) chain D residue 67 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 15) chain D residue 69 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 16) chain D residue 71 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 17) chain D residue 88 type sequence I description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 18) chain D residue 92 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 19) 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 20) 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 21) 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 22) chain D residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN D 903 source : AC3 23) chain D residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN D 903 source : AC3 24) chain D residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN C 904 source : AC4 25) chain D residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN C 904 source : AC4 26) chain D residue 154 type sequence D description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 27) chain D residue 158 type sequence K description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 28) chain D residue 37 type sequence R description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 29) chain D residue 60 type sequence C description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 30) chain D residue 67 type sequence F description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 31) chain D residue 88 type sequence I description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 32) chain D residue 92 type sequence L description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 33) chain D residue 101 type sequence T description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 34) chain D residue 103 type sequence N description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 35) chain D residue 122 type sequence R description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 36) chain D residue 157 type sequence M description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 37) chain D residue 160 type sequence L description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 38) chain D residue 162 type sequence F description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 39) chain D residue 179 type sequence M description BINDING SITE FOR RESIDUE GNB C 1004 source : AC8 40) chain D residue 60 type sequence C description BINDING SITE FOR RESIDUE BME D 204 source : BC3 41) chain D residue 62 type sequence F description BINDING SITE FOR RESIDUE BME D 204 source : BC3 42) 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 43) 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 44) 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 45) chain D residue 38 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 46) chain D residue 104 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 47) chain D residue 123 type BINDING sequence G description in other chain source Swiss-Prot : SWS_FT_FI4 48) chain D residue 157 type BINDING sequence M description in other chain source Swiss-Prot : SWS_FT_FI4 49) chain D residue 88 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 50) chain D residue 107 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 51) chain D residue 139 type MOD_RES sequence K description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 52) chain D residue 148 type MOD_RES sequence F description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 53) chain D residue 34 type catalytic sequence T description 32 source MCSA : MCSA4 54) chain D residue 100 type catalytic sequence L description 32 source MCSA : MCSA4 55) chain D residue 127 type catalytic sequence I description 32 source MCSA : MCSA4 56) chain D residue 173 type catalytic sequence I description 32 source MCSA : MCSA4 57) 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 58) 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 59) 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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