1H9A
COMPLEX OF ACTIVE MUTANT (Q365->C) OF GLUCOSE 6-PHOSPHATE DEHYDROGENASE FROM L. MESENTEROIDES WITH COENZYME NADP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004345 | molecular_function | glucose-6-phosphate dehydrogenase activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006006 | biological_process | glucose metabolic process |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0009051 | biological_process | pentose-phosphate shunt, oxidative branch |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| A | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 610 |
| Chain | Residue |
| A | HIS178 |
| A | TYR179 |
| A | LYS182 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE NAP A 799 |
| Chain | Residue |
| A | ARG46 |
| A | GLN47 |
| A | HIS84 |
| A | ASP85 |
| A | VAL86 |
| A | SER117 |
| A | VAL118 |
| A | GLU147 |
| A | LYS148 |
| A | HOH2006 |
| A | HOH2041 |
| A | HOH2189 |
| A | HOH2190 |
| A | HOH2191 |
| A | GLY12 |
| A | THR14 |
| A | GLY15 |
| A | ASP16 |
| A | LEU17 |
| A | ALA45 |
Functional Information from PROSITE/UniProt
| site_id | PS00069 |
| Number of Residues | 7 |
| Details | G6P_DEHYDROGENASE Glucose-6-phosphate dehydrogenase active site. DHYLGKE |
| Chain | Residue | Details |
| A | ASP177-GLU183 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_00966","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"9485426","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00966","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11106478","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11320304","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9485426","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00966","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"11320304","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11106478","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1dpg |
| Chain | Residue | Details |
| A | ASP177 | |
| A | HIS240 |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 843 |
| Chain | Residue | Details |
| A | ASP177 | modifies pKa |
| A | HIS178 | transition state stabiliser |
| A | HIS240 | proton acceptor, proton donor |
