3FWN
Dimeric 6-phosphogluconate dehydrogenase complexed with 6-phosphogluconate and 2'-monophosphoadenosine-5'-diphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004616 | molecular_function | phosphogluconate dehydrogenase (decarboxylating) activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0009051 | biological_process | pentose-phosphate shunt, oxidative branch |
| A | 0016054 | biological_process | organic acid catabolic process |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0019521 | biological_process | D-gluconate metabolic process |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046177 | biological_process | D-gluconate catabolic process |
| A | 0050661 | molecular_function | NADP binding |
| A | 0097216 | molecular_function | guanosine tetraphosphate binding |
| B | 0004616 | molecular_function | phosphogluconate dehydrogenase (decarboxylating) activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006098 | biological_process | pentose-phosphate shunt |
| B | 0009051 | biological_process | pentose-phosphate shunt, oxidative branch |
| B | 0016054 | biological_process | organic acid catabolic process |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0019521 | biological_process | D-gluconate metabolic process |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0046177 | biological_process | D-gluconate catabolic process |
| B | 0050661 | molecular_function | NADP binding |
| B | 0097216 | molecular_function | guanosine tetraphosphate binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE 6PG A 2002 |
| Chain | Residue |
| A | SER128 |
| A | LYS260 |
| A | ARG287 |
| A | ILE365 |
| A | HOH517 |
| A | HOH646 |
| A | HOH680 |
| A | HOH912 |
| A | HOH967 |
| B | ARG445 |
| B | PHE448 |
| A | GLY129 |
| B | HIS451 |
| A | GLY130 |
| A | LYS183 |
| A | HIS186 |
| A | ASN187 |
| A | GLU190 |
| A | TYR191 |
| A | ASN259 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE ATR B 2000 |
| Chain | Residue |
| A | ASN247 |
| B | MET11 |
| B | ALA12 |
| B | ASN33 |
| B | ARG34 |
| B | SER35 |
| B | LYS38 |
| B | VAL74 |
| B | LYS75 |
| B | GLY79 |
| B | LYS260 |
| B | HOH673 |
| B | HOH949 |
| B | HOH1098 |
| B | HOH1112 |
| B | HOH1113 |
| B | HOH1114 |
| B | HOH1408 |
| B | HOH1424 |
| B | HOH1571 |
| B | HOH1572 |
| B | HOH1669 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE 6PG B 2001 |
| Chain | Residue |
| A | ARG445 |
| A | PHE448 |
| A | HIS451 |
| B | ASN102 |
| B | SER128 |
| B | GLY129 |
| B | GLY130 |
| B | LYS183 |
| B | HIS186 |
| B | ASN187 |
| B | GLU190 |
| B | TYR191 |
| B | ASN259 |
| B | LYS260 |
| B | ARG287 |
| B | ILE365 |
| B | HOH638 |
| B | HOH692 |
| B | HOH867 |
| B | HOH1003 |
| B | HOH1577 |
Functional Information from PROSITE/UniProt
| site_id | PS00461 |
| Number of Residues | 13 |
| Details | 6PGD 6-phosphogluconate dehydrogenase signature. IlDeaANKGTGkW |
| Chain | Residue | Details |
| A | ILE253-TRP265 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:19686854 |
| Chain | Residue | Details |
| A | LYS183 | |
| B | LYS183 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000269|PubMed:19686854 |
| Chain | Residue | Details |
| A | GLU190 | |
| B | GLU190 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLY10 | |
| B | HIS451 | |
| A | ASN33 | |
| A | VAL74 | |
| A | ARG445 | |
| A | HIS451 | |
| B | GLY10 | |
| B | ASN33 | |
| B | VAL74 | |
| B | ARG445 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: in other chain |
| Chain | Residue | Details |
| A | ASN102 | |
| A | SER128 | |
| A | LYS260 | |
| A | ARG287 | |
| B | ASN102 | |
| B | SER128 | |
| B | LYS260 | |
| B | ARG287 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: in other chain => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS186 | |
| A | TYR191 | |
| B | HIS186 | |
| B | TYR191 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 2pgd |
| Chain | Residue | Details |
| A | ASN187 | |
| A | LYS183 | |
| A | GLY130 | |
| A | GLU190 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 2pgd |
| Chain | Residue | Details |
| B | ASN187 | |
| B | LYS183 | |
| B | GLY130 | |
| B | GLU190 |
