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8PIR

Crystal structure of Ser33 in complex with 3-PGA (3-phosphoglycerate)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004617molecular_functionphosphoglycerate dehydrogenase activity
A0005515molecular_functionprotein binding
A0005737cellular_componentcytoplasm
A0006564biological_processL-serine biosynthetic process
A0008652biological_processamino acid biosynthetic process
A0009070biological_processserine family amino acid biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0042802molecular_functionidentical protein binding
A0051287molecular_functionNAD binding
A0061759molecular_functionalpha-ketoglutarate reductase activity
B0004617molecular_functionphosphoglycerate dehydrogenase activity
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0006564biological_processL-serine biosynthetic process
B0008652biological_processamino acid biosynthetic process
B0009070biological_processserine family amino acid biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0042802molecular_functionidentical protein binding
B0051287molecular_functionNAD binding
B0061759molecular_functionalpha-ketoglutarate reductase activity
C0004617molecular_functionphosphoglycerate dehydrogenase activity
C0005515molecular_functionprotein binding
C0005737cellular_componentcytoplasm
C0006564biological_processL-serine biosynthetic process
C0008652biological_processamino acid biosynthetic process
C0009070biological_processserine family amino acid biosynthetic process
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0042802molecular_functionidentical protein binding
C0051287molecular_functionNAD binding
C0061759molecular_functionalpha-ketoglutarate reductase activity
F0004617molecular_functionphosphoglycerate dehydrogenase activity
F0005515molecular_functionprotein binding
F0005737cellular_componentcytoplasm
F0006564biological_processL-serine biosynthetic process
F0008652biological_processamino acid biosynthetic process
F0009070biological_processserine family amino acid biosynthetic process
F0016491molecular_functionoxidoreductase activity
F0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
F0042802molecular_functionidentical protein binding
F0051287molecular_functionNAD binding
F0061759molecular_functionalpha-ketoglutarate reductase activity
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 Residues8
DetailsACT_SITE: ACT_SITE => ECO:0000250
ChainResidueDetails
FARG287
FGLU316
AARG287
AGLU316
BARG287
BGLU316
CARG287
CGLU316

site_idSWS_FT_FI2
Number of Residues4
DetailsACT_SITE: Proton donor => ECO:0000250
ChainResidueDetails
FHIS347
AHIS347
BHIS347
CHIS347

site_idSWS_FT_FI3
Number of Residues20
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P0A9T0
ChainResidueDetails
FHIS208
AHIS347
BHIS208
BASP228
BALA285
BASP311
BHIS347
CHIS208
CASP228
CALA285
CASP311
FASP228
CHIS347
FALA285
FASP311
FHIS347
AHIS208
AASP228
AALA285
AASP311

site_idSWS_FT_FI4
Number of Residues4
DetailsMOD_RES: N-acetylserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:22814378
ChainResidueDetails
FSER2
ASER2
BSER2
CSER2

site_idSWS_FT_FI5
Number of Residues4
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:15665377, ECO:0007744|PubMed:17330950
ChainResidueDetails
FSER22
ASER22
BSER22
CSER22

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
FSER29
FSER33
ASER29
ASER33
BSER29
BSER33
CSER29
CSER33

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PDB entries from 2025-06-18

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