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6RIH

Crystal structure of PHGDH in complex with compound 9

Functional Information from GO Data
ChainGOidnamespacecontents
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue K4T A 401
ChainResidue
AGLY153
ALEU215
ATYR173
AASP174
APRO175
AILE176
AILE177
ATHR206
APRO207
ALEU209

site_idAC2
Number of Residues8
Detailsbinding site for residue SO4 B 401
ChainResidue
AARG134
BARG53
BSER54
BARG74
BALA285
BHOH520
BHOH523
BHOH543

site_idAC3
Number of Residues10
Detailsbinding site for residue K4T B 402
ChainResidue
BGLY151
BGLY153
BTYR173
BASP174
BPRO175
BILE176
BTHR206
BPRO207
BTHR212
BLEU215

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. LGILGlGRIGrevatrmqsfgmk.TIgYD
ChainResidueDetails
ALEU147-ASP174

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. IWplCDFItVHtPllpsTtgLlN
ChainResidueDetails
AILE195-ASN217

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. CKkGvRVVNcARGgIVD
ChainResidueDetails
ACYS224-ASP240

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsActive site: {"description":"Proton donor"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues20
DetailsBinding 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)"]}}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q61753","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q61753","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues4
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"PubMed","id":"25114211","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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