eF-site ID 1qh5-B PDB Code 1qh5 Chain 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 B:  MKVEVLPALTDNYMYLVIDDETKEAAIVDPVQPQKVVDAA RKHGVKLTTVLTTHHHWDHAGGNEKLVKLESGLKVYGGDD RIGALTHKITHLSTLQVGSLNVKCLATPCHTSGHICYFVS KPGGSEPPAVFTGDTLFVAGCGKFYEGTADEMCKALLEVL GRLPPDTRVYCGHEYTINNLKFARHVEPGNAAIREKLAWA KEKYSIGEPTVPSTLAEEFTYNPFMRVREKTVQQHAGETD PVTTMRAVRREKDQFKMPRD Description Functional site 1) chain B residue 54 type sequence H description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 2) chain B residue 56 type sequence H description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 3) chain B residue 110 type sequence H description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 4) chain B residue 134 type sequence D description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 5) chain B residue 58 type sequence D description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 6) chain B residue 59 type sequence H description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 7) chain B residue 173 type sequence H description BINUCLEAR ZINC BINDING SITE IN B MOLECULE source : ZNB 8) chain B residue 54 type sequence H description BINDING SITE FOR RESIDUE ZN B 261 source : AC3 9) chain B residue 56 type sequence H description BINDING SITE FOR RESIDUE ZN B 261 source : AC3 10) chain B residue 110 type sequence H description BINDING SITE FOR RESIDUE ZN B 261 source : AC3 11) chain B residue 134 type sequence D description BINDING SITE FOR RESIDUE ZN B 261 source : AC3 12) chain B residue 58 type sequence D description BINDING SITE FOR RESIDUE ZN B 262 source : AC4 13) chain B residue 59 type sequence H description BINDING SITE FOR RESIDUE ZN B 262 source : AC4 14) chain B residue 134 type sequence D description BINDING SITE FOR RESIDUE ZN B 262 source : AC4 15) chain B residue 173 type sequence H description BINDING SITE FOR RESIDUE ZN B 262 source : AC4 16) chain B residue 56 type sequence H description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 17) chain B residue 58 type sequence D description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 18) chain B residue 110 type sequence H description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 19) chain B residue 134 type sequence D description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 20) chain B residue 137 type sequence F description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 21) chain B residue 141 type sequence C description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 22) chain B residue 142 type sequence G description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 23) chain B residue 143 type sequence K description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 24) chain B residue 145 type sequence Y description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 25) chain B residue 173 type sequence H description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 26) chain B residue 175 type sequence Y description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 27) chain B residue 249 type sequence R description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 28) chain B residue 252 type sequence K description BINDING SITE FOR RESIDUE GBP B 464 source : AC6 29) chain B residue 102 type catalytic sequence V description 157 source MCSA : MCSA2 30) chain B residue 104 type catalytic sequence C description 157 source MCSA : MCSA2 31) chain B residue 106 type catalytic sequence A description 157 source MCSA : MCSA2 32) chain B residue 107 type catalytic sequence T description 157 source MCSA : MCSA2 33) chain B residue 158 type catalytic sequence E description 157 source MCSA : MCSA2 34) chain B residue 182 type catalytic sequence F description 157 source MCSA : MCSA2 35) chain B residue 221 type catalytic sequence Y description 157 source MCSA : MCSA2 36) chain B residue 104 type BINDING sequence C description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 37) chain B residue 106 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 38) chain B residue 107 type BINDING sequence T description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 39) chain B residue 158 type BINDING sequence E description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 40) chain B residue 182 type BINDING sequence F description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 41) chain B residue 191 type BINDING sequence A description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 42) chain B residue 221 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 43) chain B residue 102 type BINDING sequence V description BINDING => ECO:0000269|PubMed:10508780 source Swiss-Prot : SWS_FT_FI1 44) chain B residue 116 type MOD_RES sequence C description N6-acetyllysine => ECO:0000250|UniProtKB:Q99KB8 source Swiss-Prot : SWS_FT_FI2 45) 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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