2G76
Crystal structure of human 3-phosphoglycerate dehydrogenase
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 | 12 |
| Details | BINDING SITE FOR RESIDUE MLT A 503 |
| Chain | Residue |
| A | ARG53 |
| A | HOH511 |
| A | HOH534 |
| B | ARG134 |
| A | SER54 |
| A | ARG74 |
| A | THR77 |
| A | ASN101 |
| A | ARG235 |
| A | HIS282 |
| A | ALA285 |
| A | NAD501 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE MLT B 504 |
| Chain | Residue |
| A | ARG134 |
| B | ARG53 |
| B | SER54 |
| B | ARG74 |
| B | THR77 |
| B | ASN101 |
| B | ARG235 |
| B | HIS282 |
| B | ALA285 |
| B | NAD502 |
| B | HOH519 |
| B | HOH576 |
| site_id | AC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | THR77 |
| A | GLY151 |
| A | GLY153 |
| A | ARG154 |
| A | ILE155 |
| A | TYR173 |
| A | ASP174 |
| A | PRO175 |
| A | HIS205 |
| A | THR206 |
| A | PRO207 |
| A | SER211 |
| A | THR212 |
| A | CYS233 |
| A | ALA234 |
| A | ARG235 |
| A | ASP259 |
| A | HIS282 |
| A | GLY284 |
| A | ALA285 |
| A | MLT503 |
| A | HOH516 |
| A | HOH535 |
| A | HOH550 |
| A | HOH554 |
| A | HOH555 |
| A | HOH576 |
| A | HOH590 |
| site_id | AC4 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE NAD B 502 |
| Chain | Residue |
| A | GLU193 |
| B | THR77 |
| B | ASN101 |
| B | ALA105 |
| B | GLY151 |
| B | GLY153 |
| B | ARG154 |
| B | ILE155 |
| B | TYR173 |
| B | ASP174 |
| B | PRO175 |
| B | ILE176 |
| B | HIS205 |
| B | THR206 |
| B | PRO207 |
| B | THR212 |
| B | CYS233 |
| B | ALA234 |
| B | ARG235 |
| B | ASP259 |
| B | HIS282 |
| B | GLY284 |
| B | ALA285 |
| B | MLT504 |
| B | HOH526 |
| B | HOH557 |
| B | HOH561 |
| B | HOH570 |
| B | HOH580 |
| B | HOH582 |
| B | HOH592 |
| B | HOH602 |
| B | HOH618 |
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 | 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 | 2 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| A | GLU264 | |
| A | ASP259 | |
| A | GLY237 | |
| A | HIS282 | |
| A | ARG235 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| B | GLU264 | |
| B | ASP259 | |
| B | GLY237 | |
| B | HIS282 | |
| B | ARG235 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| A | GLU264 | |
| A | HIS282 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1gdh |
| Chain | Residue | Details |
| B | GLU264 | |
| B | HIS282 |
