6PLF
Crystal structure of human PHGDH complexed with Compound 1
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 ONV A 401 |
| Chain | Residue |
| A | TYR174 |
| A | LEU216 |
| A | HOH505 |
| A | HOH529 |
| A | HOH531 |
| A | HOH579 |
| B | GLU194 |
| A | ASP175 |
| A | PRO176 |
| A | ILE178 |
| A | HIS206 |
| A | THR207 |
| A | PRO208 |
| A | SER212 |
| A | THR213 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 402 |
| Chain | Residue |
| A | GLU242 |
| A | PHE262 |
| A | ASP269 |
| A | ARG270 |
| A | LEU272 |
| A | VAL273 |
| A | HOH509 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | LYS170 |
| A | THR171 |
| A | GLY187 |
| A | GLN189 |
| A | HOH562 |
| A | HOH573 |
| B | ASP130 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | LEU117 |
| A | GLN120 |
| A | GLN123 |
| A | ARG230 |
| A | ALA255 |
| A | HOH502 |
| A | HOH533 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue ONV B 401 |
| Chain | Residue |
| A | GLU194 |
| A | HOH529 |
| B | ARG155 |
| B | TYR174 |
| B | ASP175 |
| B | PRO176 |
| B | ILE177 |
| B | ILE178 |
| B | LEU193 |
| B | HIS206 |
| B | THR207 |
| B | PRO208 |
| B | SER212 |
| B | THR213 |
| B | LEU216 |
| B | HOH509 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | binding site for residue EDO B 402 |
| Chain | Residue |
| B | GLU242 |
| B | PRO267 |
| B | ASP269 |
| B | ARG270 |
| B | LEU272 |
| B | VAL273 |
| B | HOH599 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| B | LEU117 |
| B | GLN120 |
| B | GLN123 |
| B | ARG230 |
| B | ALA255 |
| B | ASN277 |
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 | LEU148-ASP175 |
| 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 | ILE196-ASN218 |
| 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 | CYS225-ASP241 |
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 | 20 |
| 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 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q61753","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q61753","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 4 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
