6RJ6
Crystal structure of PHGDH in complex with BI-4924
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| A | 0051287 | molecular_function | NAD binding |
| B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | binding site for residue K5K A 401 |
| Chain | Residue |
| A | GLY151 |
| A | THR206 |
| A | PRO207 |
| A | THR212 |
| A | LEU215 |
| A | HOH504 |
| A | HOH509 |
| A | ARG154 |
| A | ILE155 |
| A | TYR173 |
| A | ASP174 |
| A | PRO175 |
| A | ILE176 |
| A | ILE177 |
| A | HIS205 |
| site_id | AC2 |
| Number of Residues | 14 |
| Details | binding site for residue K5K B 401 |
| Chain | Residue |
| B | GLY151 |
| B | ILE155 |
| B | TYR173 |
| B | ASP174 |
| B | PRO175 |
| B | ILE176 |
| B | ILE177 |
| B | HIS205 |
| B | THR206 |
| B | PRO207 |
| B | SER211 |
| B | THR212 |
| B | LEU215 |
| B | HOH528 |
Functional Information from PROSITE/UniProt
| site_id | PS00065 |
| Number of Residues | 28 |
| Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. LGILGlGRIGrevatrmqsfgmk.TIgYD |
| Chain | Residue | Details |
| A | LEU147-ASP174 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. IWplCDFItVHtPllpsTtgLlN |
| Chain | Residue | Details |
| A | ILE195-ASN217 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. CKkGvRVVNcARGgIVD |
| Chain | Residue | Details |
| A | CYS224-ASP240 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Active site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton donor"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2009","submissionDatabase":"PDB data bank","title":"Crystal structure of human 3-phosphoglycerate dehydrogenase.","authoringGroup":["Structural genomics consortium (SGC)"]}}]} |
| Chain | Residue | Details |
