eF-site ID 1qh5-AB PDB Code 1qh5 Chain A, B click to enlarge Title HUMAN GLYOXALASE II WITH S-(N-HYDROXY-N-BROMOPHENYLCARBAMOYL)GLUTATHIONE Classification HYDROLASE Compound PROTEIN (HYDROXYACYLGLUTATHIONE HYDROLASE) Source Homo sapiens (Human) (GLO2_HUMAN) Sequence A:  MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAA RKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDD RIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVS KPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVL GRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWA KEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETD PVTTMRAVRREKDQFKMPRD B:  MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAA RKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDD RIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVS KPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVL GRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWA KEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETD PVTTMRAVRREKDQFKMPRD Description Functional site 1) chain A residue 54 type sequence H description BINUCLEAR ZINC BINDING SITE IN A MOLECULE source : ZNA 2) chain A residue 56 type sequence H description BINUCLEAR ZINC BINDING SITE IN A MOLECULE source : ZNA 3) chain A residue 110 type sequence H description BINUCLEAR ZINC BINDING SITE IN A MOLECULE source : ZNA 4) chain A residue 134 type sequence D description BINUCLEAR ZINC BINDING SITE IN A MOLECULE source : ZNA 5) chain A residue 58 type sequence D description BINUCLEAR ZINC BINDING SITE IN A MOLECULE source : ZNA 6) chain A residue 59 type sequence H description BINUCLEAR ZINC BINDING SITE IN A MOLECULE source : ZNA 7) chain A residue 173 type sequence H description BINUCLEAR ZINC BINDING SITE IN A MOLECULE source : ZNA 8) chain B residue 54 type sequence H description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 9) chain B residue 56 type sequence H description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 10) chain B residue 110 type sequence H description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 11) chain B residue 134 type sequence D description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 12) chain B residue 58 type sequence D description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 13) chain B residue 59 type sequence H description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 14) chain B residue 173 type sequence H description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 15) chain A residue 54 type sequence H description BINDING SITE FOR RESIDUE ZN A 261 source : AC1 16) chain A residue 56 type sequence H description BINDING SITE FOR RESIDUE ZN A 261 source : AC1 17) chain A residue 110 type sequence H description BINDING SITE FOR RESIDUE ZN A 261 source : AC1 18) chain A residue 134 type sequence D description BINDING SITE FOR RESIDUE ZN A 261 source : AC1 19) chain A residue 58 type sequence D description BINDING SITE FOR RESIDUE ZN A 262 source : AC2 20) chain A residue 59 type sequence H description BINDING SITE FOR RESIDUE ZN A 262 source : AC2 21) chain A residue 134 type sequence D description BINDING SITE FOR RESIDUE ZN A 262 source : AC2 22) chain A residue 173 type sequence H description BINDING SITE FOR RESIDUE ZN A 262 source : AC2 23) chain B residue 54 type sequence H description BINDING SITE FOR RESIDUE ZN B 261 source : AC3 24) chain B residue 56 type sequence H description BINDING SITE FOR RESIDUE ZN B 261 source : AC3 25) chain B residue 110 type sequence H description BINDING SITE FOR RESIDUE ZN B 261 source : AC3 26) chain B residue 134 type sequence D description BINDING SITE FOR RESIDUE ZN B 261 source : AC3 27) chain B residue 58 type sequence D description BINDING SITE FOR RESIDUE ZN B 262 source : AC4 28) chain B residue 59 type sequence H description BINDING SITE FOR RESIDUE ZN B 262 source : AC4 29) chain B residue 134 type sequence D description BINDING SITE FOR RESIDUE ZN B 262 source : AC4 30) chain B residue 173 type sequence H description BINDING SITE FOR RESIDUE ZN B 262 source : AC4 31) chain A residue 58 type sequence D description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 32) chain A residue 110 type sequence H description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 33) chain A residue 134 type sequence D description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 34) chain A residue 137 type sequence F description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 35) chain A residue 141 type sequence C description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 36) chain A residue 142 type sequence G description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 37) chain A residue 143 type sequence K description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 38) chain A residue 145 type sequence Y description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 39) chain A residue 173 type sequence H description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 40) chain A residue 175 type sequence Y description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 41) chain A residue 249 type sequence R description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 42) chain A residue 252 type sequence K description BINDING SITE FOR RESIDUE GSH A 463 source : AC5 43) chain B residue 56 type sequence H description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 44) chain B residue 58 type sequence D description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 45) chain B residue 110 type sequence H description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 46) chain B residue 134 type sequence D description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 47) chain B residue 137 type sequence F description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 48) chain B residue 141 type sequence C description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 49) chain B residue 142 type sequence G description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 50) chain B residue 143 type sequence K description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 51) chain B residue 145 type sequence Y description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 52) chain B residue 173 type sequence H description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 53) chain B residue 175 type sequence Y description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 54) chain B residue 249 type sequence R description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 55) chain B residue 252 type sequence K description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 56) chain A residue 102 type catalytic sequence V description 157 source MCSA : MCSA1 57) chain A residue 104 type catalytic sequence C description 157 source MCSA : MCSA1 58) chain A residue 106 type catalytic sequence A description 157 source MCSA : MCSA1 59) chain A residue 107 type catalytic sequence T description 157 source MCSA : MCSA1 60) chain A residue 158 type catalytic sequence E description 157 source MCSA : MCSA1 61) chain A residue 182 type catalytic sequence F description 157 source MCSA : MCSA1 62) chain A residue 221 type catalytic sequence Y description 157 source MCSA : MCSA1 63) chain B residue 102 type catalytic sequence V description 157 source MCSA : MCSA2 64) chain B residue 104 type catalytic sequence C description 157 source MCSA : MCSA2 65) chain B residue 106 type catalytic sequence A description 157 source MCSA : MCSA2 66) chain B residue 107 type catalytic sequence T description 157 source MCSA : MCSA2 67) chain B residue 158 type catalytic sequence E description 157 source MCSA : MCSA2 68) chain B residue 182 type catalytic sequence F description 157 source MCSA : MCSA2 69) chain B residue 221 type catalytic sequence Y description 157 source MCSA : MCSA2 70) chain A residue 102 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 71) chain B residue 104 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 72) chain B residue 106 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 73) chain B residue 107 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 74) chain B residue 158 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 75) chain B residue 182 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 76) chain B residue 191 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 77) chain B residue 221 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 78) chain A residue 104 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 79) chain A residue 106 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 80) chain A residue 107 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 81) chain A residue 158 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 82) chain A residue 182 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 83) chain A residue 191 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 84) chain A residue 221 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 85) chain B residue 102 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 86) chain A residue 116 type MOD_RES sequence C description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KB8 source Swiss-Prot : SWS_FT_FI2 87) chain B residue 116 type MOD_RES sequence C description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KB8 source Swiss-Prot : SWS_FT_FI2 88) chain A residue 229 type MOD_RES sequence E description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KB8 source Swiss-Prot : SWS_FT_FI3 89) chain B residue 229 type MOD_RES sequence E description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KB8 source Swiss-Prot : SWS_FT_FI3

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