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2O4C

Crystal Structure of D-Erythronate-4-phosphate Dehydrogenase Complexed with NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008615biological_processpyridoxine biosynthetic process
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0033711molecular_function4-phosphoerythronate dehydrogenase activity
A0036001biological_process'de novo' pyridoxal 5'-phosphate biosynthetic process
A0046983molecular_functionprotein dimerization activity
A0051287molecular_functionNAD binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008615biological_processpyridoxine biosynthetic process
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0033711molecular_function4-phosphoerythronate dehydrogenase activity
B0036001biological_process'de novo' pyridoxal 5'-phosphate biosynthetic process
B0046983molecular_functionprotein dimerization activity
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE PO4 A 900
ChainResidue
AARG44
ASER45
ATHR66
ATYR258
AARG346

site_idAC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE NAD B 1001
ChainResidue
BGLY125
BGLN126
BVAL127
BCYS145
BASP146
BPRO147
BPRO148
BHIS174
BTHR175
BPRO176
BHIS183
BTHR185
BALA206
BSER207
BARG208
BASP232
BHIS254
BALA256
BGLY257
BHOH2652
BHOH2661
BHOH2702
BASN91
BVAL95
BVAL122
BGLY123

site_idAC3
Number of Residues28
DetailsBINDING SITE FOR RESIDUE NAD A 1002
ChainResidue
AASN91
AVAL95
AGLY123
AGLY125
AGLN126
AVAL127
ACYS145
AASP146
APRO147
APRO148
AHIS174
ATHR175
APRO176
AHIS183
ATHR185
AALA206
ASER207
AARG208
AASP232
AHIS254
AALA256
AGLY257
AHOH1003
AHOH1004
AHOH1008
AHOH1038
AHOH1060
AHOH1084

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE TLA B 500
ChainResidue
BARG208
BHIS254
BTYR258
BARG346

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 2647
ChainResidue
BLEU138
BTRP140
BALA307
BHOH2676

Functional Information from PROSITE/UniProt
site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. LRpGtWLVNaSRGaVVD
ChainResidueDetails
ALEU197-ASP213

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: ACT_SITE => ECO:0000255|HAMAP-Rule:MF_01825, ECO:0000305|PubMed:17217963
ChainResidueDetails
AARG208
AGLU237
BARG208
BGLU237

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_01825, ECO:0000305|PubMed:17217963
ChainResidueDetails
AHIS254
BHIS254

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01825, ECO:0000305|PubMed:17217963
ChainResidueDetails
ASER45
ATHR66
ATYR258
BSER45
BTHR66
BTYR258

site_idSWS_FT_FI4
Number of Residues12
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01825, ECO:0000269|PubMed:17217963
ChainResidueDetails
AGLN126
BALA206
BASP232
BGLY257
AASP146
ATHR175
AALA206
AASP232
AGLY257
BGLN126
BASP146
BTHR175

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1psd
ChainResidueDetails
AHIS254
AGLU237

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1psd
ChainResidueDetails
BHIS254
BGLU237

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PDB entries from 2025-06-18

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