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2PA3

crystal structure of serine bound G336V mutant of E.coli phosphoglycerate dehydrogenase

Functional Information from GO Data
ChainGOidnamespacecontents
A0004617molecular_functionphosphoglycerate dehydrogenase activity
A0005829cellular_componentcytosol
A0006564biological_processL-serine 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
A0047545molecular_function2-hydroxyglutarate dehydrogenase activity
A0051287molecular_functionNAD binding
A0070403molecular_functionNAD+ binding
A0070404molecular_functionNADH binding
A0070905molecular_functionserine binding
Functional Information from PDB Data
site_idAC1
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SER A 451
ChainResidue
AHIS344
AASN346
AARG347
APRO348
AGLY349
ALEU351
AASN364
AILE365
AHOH467

site_idAC2
Number of Residues25
DetailsBINDING SITE FOR RESIDUE NAI A 450
ChainResidue
AILE84
APHE106
AASN108
AVAL112
ATYR159
AGLY160
AHIS161
AILE162
ATYR180
AASP181
AILE182
ALYS185
AHIS210
AVAL211
APRO212
ASER216
ATHR217
AMET220
AALA238
ASER239
AARG240
AASP264
AHIS292
AGLY294
AGLY295

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. LGIIGyGHIGtqlgilaeslgmy.VYfYD
ChainResidueDetails
ALEU154-ASP181

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LLnmSDVVsLHvPenpsTknMmG
ChainResidueDetails
ALEU200-GLY222

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKpGsLLINaSRGtVVD
ChainResidueDetails
AMET229-ASP245

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE:
ChainResidueDetails
AARG240
AGLU269

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Proton donor
ChainResidueDetails
AHIS292

site_idSWS_FT_FI3
Number of Residues5
DetailsBINDING: BINDING => ECO:0000269|PubMed:7719856
ChainResidueDetails
AHIS161
AASP181
AALA238
AASP264
AHIS292

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1psd
ChainResidueDetails
AGLU269
AHIS292

site_idMCSA1
Number of Residues2
DetailsM-CSA 785
ChainResidueDetails
AGLU269electrostatic stabiliser
AHIS292proton acceptor, proton donor

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PDB entries from 2024-10-02

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