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8PIO

Crystal structure of Ser33 in complex with PHP (3-phosphohydroxypyruvate)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004617molecular_functionphosphoglycerate dehydrogenase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006564biological_processL-serine biosynthetic process
A0006979biological_processresponse to oxidative stress
A0009070biological_processserine family amino acid biosynthetic process
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0040029biological_processepigenetic regulation of gene expression
A0042802molecular_functionidentical protein binding
A0051287molecular_functionNAD binding
A0120568molecular_function(R)-2-hydroxyglutarate (NAD+) dehydrogenase activity
A1902494cellular_componentcatalytic complex
B0004617molecular_functionphosphoglycerate dehydrogenase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006564biological_processL-serine biosynthetic process
B0006979biological_processresponse to oxidative stress
B0009070biological_processserine family amino acid biosynthetic process
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0040029biological_processepigenetic regulation of gene expression
B0042802molecular_functionidentical protein binding
B0051287molecular_functionNAD binding
B0120568molecular_function(R)-2-hydroxyglutarate (NAD+) dehydrogenase activity
B1902494cellular_componentcatalytic complex
C0004617molecular_functionphosphoglycerate dehydrogenase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0005829cellular_componentcytosol
C0006564biological_processL-serine biosynthetic process
C0006979biological_processresponse to oxidative stress
C0009070biological_processserine family amino acid biosynthetic process
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0040029biological_processepigenetic regulation of gene expression
C0042802molecular_functionidentical protein binding
C0051287molecular_functionNAD binding
C0120568molecular_function(R)-2-hydroxyglutarate (NAD+) dehydrogenase activity
C1902494cellular_componentcatalytic complex
F0004617molecular_functionphosphoglycerate dehydrogenase activity
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0005829cellular_componentcytosol
F0006564biological_processL-serine biosynthetic process
F0006979biological_processresponse to oxidative stress
F0009070biological_processserine family amino acid biosynthetic process
F0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F0040029biological_processepigenetic regulation of gene expression
F0042802molecular_functionidentical protein binding
F0051287molecular_functionNAD binding
F0120568molecular_function(R)-2-hydroxyglutarate (NAD+) dehydrogenase activity
F1902494cellular_componentcatalytic complex
Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. LGIIGyGHIGsqlsvlaeamglh.VLyYD
ChainResidueDetails
FLEU201-ASP228

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LLnkSDFVtLHvPatpeTekMlS
ChainResidueDetails
FLEU247-SER269

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKdGaYVINaSRGtVVD
ChainResidueDetails
FMET276-ASP292

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues280
DetailsDomain: {"description":"ACT","evidences":[{"source":"PROSITE-ProRule","id":"PRU01007","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsActive site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues32
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P0A9T0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15665377","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

253795

PDB entries from 2026-05-20

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