eF-site ID 1fro-C PDB Code 1fro Chain C click to enlarge Title HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR Classification LACTOYLGLUTATHIONE LYASE Compound LACTOYLGLUTATHIONE LYASE Source Homo sapiens (Human) (LGUL_HUMAN) Sequence C:  GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDF YTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEK IAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHI GIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPD GYWIEILNPNKMATLM Description Functional site 1) chain C residue 33 type sequence Q description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN3 2) chain C residue 99 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN3 3) chain C residue 126 type sequence H description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN4 4) chain C residue 172 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN4 5) chain C residue 60 type sequence C description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 6) chain C residue 62 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 7) chain C residue 65 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 8) chain C residue 67 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 9) chain C residue 69 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 10) chain C residue 71 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 11) chain C residue 88 type sequence I description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 12) chain C residue 92 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD4 13) chain C residue 157 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 14) chain C residue 160 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 15) chain C residue 162 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 16) chain C residue 174 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 17) chain C residue 179 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 18) chain C residue 183 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD5 19) 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 20) 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 21) 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 22) chain C residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN C 201 source : AC3 23) chain C residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN C 201 source : AC3 24) chain C residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN D 201 source : AC4 25) chain C residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN D 201 source : AC4 26) chain C residue 17 type sequence S description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 27) chain C residue 122 type sequence R description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 28) chain C residue 150 type sequence K description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 29) chain C residue 157 type sequence M description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 30) chain C residue 162 type sequence F description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 31) chain C residue 172 type sequence E description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 32) chain C residue 183 type sequence M description BINDING SITE FOR RESIDUE GSB C 200 source : AC7 33) chain C residue 37 type sequence R description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 34) chain C residue 62 type sequence F description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 35) chain C residue 67 type sequence F description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 36) chain C residue 101 type sequence T description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 37) chain C residue 103 type sequence N description BINDING SITE FOR RESIDUE GSB D 200 source : AC8 38) chain C residue 33 type catalytic sequence Q description 32 source MCSA : MCSA3 39) chain C residue 99 type catalytic sequence E description 32 source MCSA : MCSA3 40) chain C residue 126 type catalytic sequence H description 32 source MCSA : MCSA3 41) chain C residue 172 type catalytic sequence E description 32 source MCSA : MCSA3 42) 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 43) chain C residue 147 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 44) 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 45) 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 46) chain C residue 37 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 47) chain C residue 103 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 48) chain C residue 122 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI4 49) chain C residue 156 type BINDING sequence K description in other chain source Swiss-Prot : SWS_FT_FI4 50) 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 51) 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 52) chain C residue 87 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 53) chain C residue 106 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 54) chain C 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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