eF-site ID 1qh3-A PDB Code 1qh3 Chain A click to enlarge Title HUMAN GLYOXALASE II WITH CACODYLATE AND ACETATE IONS PRESENT IN THE ACTIVE SITE Classification HYDROLASE Compound PROTEIN (HYDROXYACYLGLUTATHIONE HYDROLASE) Source Homo sapiens (Human) (GLO2_HUMAN) Sequence A:  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 A residue 54 type sequence H description BINDING SITE FOR RESIDUE ZN A 261 source : AC1 9) chain A residue 56 type sequence H description BINDING SITE FOR RESIDUE ZN A 261 source : AC1 10) chain A residue 110 type sequence H description BINDING SITE FOR RESIDUE ZN A 261 source : AC1 11) chain A residue 134 type sequence D description BINDING SITE FOR RESIDUE ZN A 261 source : AC1 12) chain A residue 58 type sequence D description BINDING SITE FOR RESIDUE ZN A 262 source : AC2 13) chain A residue 59 type sequence H description BINDING SITE FOR RESIDUE ZN A 262 source : AC2 14) chain A residue 134 type sequence D description BINDING SITE FOR RESIDUE ZN A 262 source : AC2 15) chain A residue 173 type sequence H description BINDING SITE FOR RESIDUE ZN A 262 source : AC2 16) chain A residue 56 type sequence H description BINDING SITE FOR RESIDUE CAC A 463 source : AC3 17) chain A residue 58 type sequence D description BINDING SITE FOR RESIDUE CAC A 463 source : AC3 18) chain A residue 110 type sequence H description BINDING SITE FOR RESIDUE CAC A 463 source : AC3 19) chain A residue 134 type sequence D description BINDING SITE FOR RESIDUE CAC A 463 source : AC3 20) chain A residue 145 type sequence Y description BINDING SITE FOR RESIDUE CAC A 463 source : AC3 21) chain A residue 173 type sequence H description BINDING SITE FOR RESIDUE CAC A 463 source : AC3 22) chain A residue 137 type sequence F description BINDING SITE FOR RESIDUE ACT A 464 source : AC4 23) chain A residue 141 type sequence C description BINDING SITE FOR RESIDUE ACT A 464 source : AC4 24) chain A residue 143 type sequence K description BINDING SITE FOR RESIDUE ACT A 464 source : AC4 25) chain A residue 175 type sequence Y description BINDING SITE FOR RESIDUE ACT A 464 source : AC4 26) chain A residue 249 type sequence R description BINDING SITE FOR RESIDUE ACT A 464 source : AC4 27) chain A residue 252 type sequence K description BINDING SITE FOR RESIDUE ACT A 464 source : AC4 28) chain A residue 153 type sequence C description BINDING SITE FOR RESIDUE CAC A 265 source : AC5 29) chain A residue 158 type sequence E description BINDING SITE FOR RESIDUE CAC A 265 source : AC5 30) chain A residue 185 type sequence H description BINDING SITE FOR RESIDUE MN A 266 source : AC6 31) chain A residue 235 type sequence H description BINDING SITE FOR RESIDUE MN A 266 source : AC6 32) chain A residue 251 type sequence E description BINDING SITE FOR RESIDUE MN A 266 source : AC6 33) chain A residue 102 type catalytic sequence V description 157 source MCSA : MCSA1 34) chain A residue 104 type catalytic sequence C description 157 source MCSA : MCSA1 35) chain A residue 106 type catalytic sequence A description 157 source MCSA : MCSA1 36) chain A residue 107 type catalytic sequence T description 157 source MCSA : MCSA1 37) chain A residue 158 type catalytic sequence E description 157 source MCSA : MCSA1 38) chain A residue 182 type catalytic sequence F description 157 source MCSA : MCSA1 39) chain A residue 221 type catalytic sequence Y description 157 source MCSA : MCSA1 40) chain A residue 229 type MOD_RES sequence E description N6-succinyllysine; alternate => ECO:0000250|UniProtKB:Q99KB8 source Swiss-Prot : SWS_FT_FI3 41) chain A residue 102 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 42) chain A residue 104 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 43) chain A residue 106 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 44) chain A residue 107 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 45) chain A residue 158 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 46) chain A residue 182 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 47) chain A residue 191 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 221 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 49) chain A residue 116 type MOD_RES sequence C description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KB8 source Swiss-Prot : SWS_FT_FI2

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