eF-site ID 1fro-B PDB Code 1fro Chain B click to enlarge Title HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR Classification LACTOYLGLUTATHIONE LYASE Compound LACTOYLGLUTATHIONE LYASE Source Homo sapiens (Human) (LGUL_HUMAN) Sequence B:  GGLTDEAALSCCSDADPSTKDFLLQQTMLRVKDPKKSLDF YTRVLGMTLIQKCDFPIMKFSLYFLAYEDKNDIPKEKDEK IAWALSRKATLELTHNWGTEDDETQSYHNGNSDPRGFGHI GIAVPDVYSACKRFEELGVKFVKKPDDGKMKGLAFIQDPD GYWIEILNPNKMATLM Description Functional site 1) chain B residue 126 type sequence H description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN1 2) chain B residue 172 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN1 3) chain B residue 33 type sequence Q description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN2 4) chain B residue 99 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN2 5) chain B residue 157 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 6) chain B residue 160 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 7) chain B residue 162 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 8) chain B residue 174 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 9) chain B residue 179 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 10) chain B residue 183 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 11) chain B residue 60 type sequence C description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 12) chain B residue 62 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 13) chain B residue 65 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 14) chain B residue 67 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 15) chain B residue 69 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 16) chain B residue 71 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 17) chain B residue 88 type sequence I description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 18) chain B residue 92 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 19) 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 20) 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 21) 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 22) chain B residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 23) chain B residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 24) chain B residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN B 201 source : AC2 25) chain B residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN B 201 source : AC2 26) chain B residue 37 type sequence R description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 27) chain B residue 62 type sequence F description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 28) chain B residue 67 type sequence F description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 29) chain B residue 101 type sequence T description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 30) chain B residue 103 type sequence N description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 31) chain B residue 122 type sequence R description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 32) chain B residue 150 type sequence K description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 33) chain B residue 157 type sequence M description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 34) chain B residue 162 type sequence F description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 35) chain B residue 172 type sequence E description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 36) chain B residue 183 type sequence M description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 37) chain B residue 33 type catalytic sequence Q description 32 source MCSA : MCSA2 38) chain B residue 99 type catalytic sequence E description 32 source MCSA : MCSA2 39) chain B residue 126 type catalytic sequence H description 32 source MCSA : MCSA2 40) chain B residue 172 type catalytic sequence E description 32 source MCSA : MCSA2 41) 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 42) 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 43) 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 44) chain B residue 147 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 45) 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 46) 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 47) chain B residue 106 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 48) chain B residue 138 type MOD_RES sequence C description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 49) chain B residue 37 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 50) chain B residue 103 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 51) chain B residue 122 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI4 52) chain B residue 156 type BINDING sequence K description in other chain source Swiss-Prot : SWS_FT_FI4 53) chain B residue 87 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7

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