eF-site ID 1qin-B PDB Code 1qin Chain B click to enlarge Title HUMAN GLYOXALASE I COMPLEXED WITH S-(N-HYDROXY-N-P-IODOPHENYLCARBAMOYL) GLUTATHIONE Classification LYASE Compound PROTEIN (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 B 301 source : AC1 23) chain B residue 99 type sequence E description BINDING SITE FOR RESIDUE ZN B 301 source : AC1 24) chain B residue 126 type sequence H description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 25) chain B residue 172 type sequence E description BINDING SITE FOR RESIDUE ZN A 401 source : AC2 26) chain B residue 33 type sequence Q description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 27) chain B residue 37 type sequence R description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 28) chain B residue 67 type sequence F description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 29) chain B residue 69 type sequence L description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 30) chain B residue 71 type sequence F description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 31) chain B residue 99 type sequence E description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 32) chain B residue 101 type sequence T description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 33) chain B residue 103 type sequence N description BINDING SITE FOR RESIDUE GIP A 300 source : AC3 34) chain B residue 122 type sequence R description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 35) chain B residue 126 type sequence H description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 36) chain B residue 150 type sequence K description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 37) chain B residue 155 type sequence G description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 38) chain B residue 156 type sequence K description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 39) chain B residue 157 type sequence M description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 40) chain B residue 160 type sequence L description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 41) chain B residue 162 type sequence F description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 42) chain B residue 172 type sequence E description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 43) chain B residue 179 type sequence M description BINDING SITE FOR RESIDUE GIP B 400 source : AC4 44) chain B residue 34 type catalytic sequence T description 32 source MCSA : MCSA2 45) chain B residue 100 type catalytic sequence L description 32 source MCSA : MCSA2 46) chain B residue 127 type catalytic sequence I description 32 source MCSA : MCSA2 47) chain B residue 173 type catalytic sequence I description 32 source MCSA : MCSA2 48) chain B 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 49) chain B 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 50) chain B 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 51) chain B residue 38 type BINDING sequence V description source Swiss-Prot : SWS_FT_FI3 52) chain B residue 104 type BINDING sequence W description source Swiss-Prot : SWS_FT_FI3 53) chain B residue 123 type BINDING sequence G description in other chain source Swiss-Prot : SWS_FT_FI4 54) chain B residue 157 type BINDING sequence M description in other chain source Swiss-Prot : SWS_FT_FI4 55) chain B residue 148 type MOD_RES sequence F description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI10 56) chain B 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 57) chain B 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 58) chain B residue 88 type MOD_RES sequence I description N6-succinyllysine => ECO:0000250|UniProtKB:Q9CPU0 source Swiss-Prot : SWS_FT_FI7 59) chain B residue 107 type MOD_RES sequence E description Phosphothreonine => ECO:0000269|PubMed:19199007 source Swiss-Prot : SWS_FT_FI8 60) chain B residue 139 type MOD_RES sequence K description S-glutathionyl cysteine; alternate => ECO:0000269|PubMed:20454679 source Swiss-Prot : SWS_FT_FI9

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