Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004616 | molecular_function | phosphogluconate dehydrogenase (decarboxylating) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019521 | biological_process | D-gluconate metabolic process |
| A | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 505 |
| Chain | Residue |
| A | TYR191 |
| A | GLN259 |
| A | LYS260 |
| A | ARG287 |
| A | ARG446 |
| A | HIS452 |
| A | HOH528 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 507 |
| Chain | Residue |
| A | ASN187 |
| A | HOH613 |
| A | HOH614 |
| A | HOH1658 |
| A | ASN102 |
| A | LYS183 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 508 |
| Chain | Residue |
| A | LYS50 |
| A | GLY211 |
| A | HIS212 |
| A | HIS248 |
| A | HOH524 |
| A | HOH636 |
| A | HOH899 |
| A | HOH1120 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE 2AM A 500 |
| Chain | Residue |
| A | ASN32 |
| A | ARG33 |
| A | THR34 |
| A | VAL74 |
| A | LYS75 |
| A | ALA79 |
| A | PHE83 |
Functional Information from PROSITE/UniProt
| site_id | PS00461 |
| Number of Residues | 13 |
| Details | 6PGD 6-phosphogluconate dehydrogenase signature. IrDsaGQKGTGkW |
| Chain | Residue | Details |
| A | ILE253-TRP265 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"description":"in other chain"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DCD0","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9DCD0","evidenceCode":"ECO:0000250"}]} |
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 | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 889 |
| Chain | Residue | Details |
| A | SER128 | electrostatic stabiliser, promote heterolysis |
| A | LYS183 | proton acceptor, proton donor |
| A | HIS186 | electrostatic stabiliser, promote heterolysis |
| A | ASN187 | electrostatic stabiliser, promote heterolysis |
| A | GLU190 | proton acceptor, proton donor |
