eF-site ID 1fro-A PDB Code 1fro Chain A click to enlarge Title HUMAN GLYOXALASE I WITH BENZYL-GLUTATHIONE INHIBITOR Classification LACTOYLGLUTATHIONE LYASE Compound LACTOYLGLUTATHIONE LYASE Source Homo sapiens (Human) (LGUL_HUMAN) Sequence A:  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 A residue 126 type sequence H description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN2 4) chain A residue 172 type sequence E description ZINC BINDING SITE AT DIMER INTERFACE. source : ZN2 5) chain A residue 60 type sequence C description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 6) chain A residue 62 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 7) chain A residue 65 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 8) chain A residue 67 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 9) chain A residue 69 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 10) chain A residue 71 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 11) chain A residue 88 type sequence I description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 12) chain A residue 92 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD2 13) chain A residue 157 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 14) chain A residue 160 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 15) chain A residue 162 type sequence F description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 16) chain A residue 174 type sequence L description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 17) chain A residue 179 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 18) chain A residue 183 type sequence M description HYDROPHOBIC SUBSTRATE BINDING POCKET AT DIMER INTERFACE. source : HD3 19) 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 20) 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 21) 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 22) chain A residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 23) chain A residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN A 201 source : AC1 24) chain A residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN B 201 source : AC2 25) chain A residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN B 201 source : AC2 26) chain A residue 122 type sequence R description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 27) chain A residue 150 type sequence K description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 28) chain A residue 157 type sequence M description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 29) chain A residue 162 type sequence F description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 30) chain A residue 172 type sequence E description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 31) chain A residue 183 type sequence M description BINDING SITE FOR RESIDUE GSB A 200 source : AC5 32) chain A residue 37 type sequence R description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 33) chain A residue 62 type sequence F description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 34) chain A residue 67 type sequence F description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 35) chain A residue 101 type sequence T description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 36) chain A residue 103 type sequence N description BINDING SITE FOR RESIDUE GSB B 200 source : AC6 37) chain A residue 33 type catalytic sequence Q description 32 source MCSA : MCSA1 38) chain A residue 99 type catalytic sequence E description 32 source MCSA : MCSA1 39) chain A residue 126 type catalytic sequence H description 32 source MCSA : MCSA1 40) chain A residue 172 type catalytic sequence E description 32 source MCSA : MCSA1 41) 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 42) 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 43) 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 44) chain A residue 147 type MOD_RES sequence K description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 45) 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 46) 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 47) chain A residue 106 type MOD_RES sequence T description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 48) chain A residue 138 type MOD_RES sequence C description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 49) chain A residue 33-54 type prosite sequence QTMLRVKDPKKSLDFYTRVLGM description GLYOXALASE_I_1 Glyoxalase I signature 1. QTmLrVkdpkKSldFYtrvLGM source prosite : PS00934 50) chain A residue 117-133 type prosite sequence GNSDPRGFGHIGIAVPD description GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD source prosite : PS00935 51) chain A residue 37 type BINDING sequence R description source Swiss-Prot : SWS_FT_FI3 52) chain A residue 103 type BINDING sequence N description source Swiss-Prot : SWS_FT_FI3 53) chain A residue 122 type BINDING sequence R description in other chain source Swiss-Prot : SWS_FT_FI4 54) chain A residue 156 type BINDING sequence K description in other chain source Swiss-Prot : SWS_FT_FI4 55) chain A residue 87 type MOD_RES sequence K description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7

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