eF-site ID 1qip-A PDB Code 1qip Chain A click to enlarge Title HUMAN GLYOXALASE I COMPLEXED WITH S-P-NITROBENZYLOXYCARBONYLGLUTATHIONE Classification LYASE Compound PROTEIN (LACTOYLGLUTATHIONE LYASE) Source null (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 B 901 source : AC1 23) chain A residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN B 901 source : AC1 24) chain A residue 33 type sequence Q description BINDING SITE FOR RESIDUE ZN A 902 source : AC2 25) chain A residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN A 902 source : AC2 26) chain A residue 122 type sequence R description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 27) chain A residue 160 type sequence L description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 28) chain A residue 162 type sequence F description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 29) chain A residue 172 type sequence E description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 30) chain A residue 179 type sequence M description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 31) chain A residue 182 type sequence L description BINDING SITE FOR RESIDUE GNB B 1001 source : AC5 32) chain A residue 37 type sequence R description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 33) chain A residue 58 type sequence Q description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 34) chain A residue 60 type sequence C description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 35) chain A residue 67 type sequence F description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 36) chain A residue 71 type sequence F description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 37) chain A residue 88 type sequence I description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 38) chain A residue 92 type sequence L description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 39) chain A residue 101 type sequence T description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 40) chain A residue 103 type sequence N description BINDING SITE FOR RESIDUE GNB A 1002 source : AC6 41) chain A residue 17 type sequence S description BINDING SITE FOR RESIDUE GNB D 1003 source : AC7 42) chain A residue 58 type sequence Q description BINDING SITE FOR RESIDUE BME A 204 source : AC9 43) chain A residue 59 type sequence K description BINDING SITE FOR RESIDUE BME A 204 source : AC9 44) chain A residue 60 type sequence C description BINDING SITE FOR RESIDUE BME A 204 source : AC9 45) chain A residue 62 type sequence F description BINDING SITE FOR RESIDUE BME A 204 source : AC9 46) 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 47) 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 48) 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 49) chain A residue 38 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 50) chain A residue 104 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 51) chain A residue 123 type BINDING sequence G description in other chain source Swiss-Prot : SWS_FT_FI4 52) chain A residue 157 type BINDING sequence M description in other chain source Swiss-Prot : SWS_FT_FI4 53) chain A residue 88 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 54) chain A residue 107 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 55) chain A residue 139 type MOD_RES sequence K description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9 56) chain A residue 148 type MOD_RES sequence F description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 57) chain A residue 34 type catalytic sequence T description 32 source MCSA : MCSA1 58) chain A residue 100 type catalytic sequence L description 32 source MCSA : MCSA1 59) chain A residue 127 type catalytic sequence I description 32 source MCSA : MCSA1 60) chain A residue 173 type catalytic sequence I description 32 source MCSA : MCSA1 61) chain A residue 33-54 type prosite sequence QTMLRVKDPKKSLDFYTRVLGM description GLYOXALASE_I_1 Glyoxalase I signature 1. QTmLrVkdpkKSldFYtrvLGM source prosite : PS00934 62) chain A residue 117-133 type prosite sequence GNSDPRGFGHIGIAVPD description GLYOXALASE_I_2 Glyoxalase I signature 2. GNsdpr.GFGHIGiAvpD source prosite : PS00935 63) 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 64) 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

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