4GWK
Crystal structure of 6-phosphogluconate dehydrogenase complexed with 3-phosphoglyceric acid
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004616 | molecular_function | phosphogluconate dehydrogenase (decarboxylating) activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006098 | biological_process | pentose-phosphate shunt |
| A | 0006739 | biological_process | NADP+ metabolic process |
| A | 0006740 | biological_process | NADPH regeneration |
| A | 0009051 | biological_process | pentose-phosphate shunt, oxidative branch |
| A | 0019521 | biological_process | D-gluconate metabolic process |
| A | 0030246 | molecular_function | carbohydrate binding |
| A | 0031406 | molecular_function | carboxylic acid binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0070062 | cellular_component | extracellular exosome |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE 3PG A 501 |
| Chain | Residue |
| A | ALA212 |
| A | GLN213 |
| A | LYS248 |
| A | HIS249 |
| A | PRO252 |
| A | HOH682 |
| A | HOH757 |
| A | HOH895 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MES A 502 |
| Chain | Residue |
| A | ARG107 |
| A | MET185 |
| A | TRP266 |
| A | HOH625 |
| A | HOH639 |
| A | HOH689 |
| A | GLU105 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MES A 503 |
| Chain | Residue |
| A | GLY131 |
| A | GLU132 |
| A | GLY167 |
| A | GLU168 |
| A | GLY451 |
| A | ALA452 |
| site_id | AC4 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE 3PG A 504 |
| Chain | Residue |
| A | GLU191 |
| A | TYR192 |
| A | LYS261 |
| A | GLY262 |
| A | THR263 |
| A | ARG288 |
| A | ARG447 |
| A | HOH628 |
| A | HOH651 |
| A | HOH793 |
| A | HOH817 |
Functional Information from PROSITE/UniProt
| site_id | PS00461 |
| Number of Residues | 13 |
| Details | 6PGD 6-phosphogluconate dehydrogenase signature. IrDsaGQKGTGkW |
| Chain | Residue | Details |
| A | ILE254-TRP266 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"description":"in other chain","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2009","submissionDatabase":"PDB data bank","title":"Structure of human phosphogluconate dehydrogenase in complex with NADPH at 2.53 A.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 7 |
| Details | Binding site: {"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9DCD0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9DCD0","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
