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3NAQ

Apo-form of NAD-dependent formate dehydrogenase from higher-plant Arabidopsis thaliana

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0008863molecular_functionformate dehydrogenase (NAD+) activity
A0009507cellular_componentchloroplast
A0009536cellular_componentplastid
A0009579cellular_componentthylakoid
A0009611biological_processresponse to wounding
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0032787biological_processmonocarboxylic acid metabolic process
A0042183biological_processformate catabolic process
A0051287molecular_functionNAD binding
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0008863molecular_functionformate dehydrogenase (NAD+) activity
B0009507cellular_componentchloroplast
B0009536cellular_componentplastid
B0009579cellular_componentthylakoid
B0009611biological_processresponse to wounding
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0032787biological_processmonocarboxylic acid metabolic process
B0042183biological_processformate catabolic process
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AARG354
APRO362
AHOH396
AHOH479

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 18
ChainResidue
AGLU359
AASP360
AHOH418
AHOH581

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 20
ChainResidue
AARG185
BLYS45
ATYR184

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 2
ChainResidue
BARG354
BHOH432
BHOH549

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 3
ChainResidue
BGLU359
BASP360
BHOH455

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 19
ChainResidue
BTYR184
BARG185
BASN326
BHOH558

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IGTVGaGRIGklllqrlkpfgcn.LLyHD
ChainResidueDetails
AILE194-ASP221

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MLpkCDVIvINmPltekTrgMfN
ChainResidueDetails
AMET244-ASN266

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. LKkGvLIVNnARGaIME
ChainResidueDetails
ALEU273-GLU289

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues22
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2010","submissionDatabase":"PDB data bank","title":"Structures of the apo and holo forms of NAD-dependent formate dehydrogenase from the higher-plant Arabidopsis thaliana.","authors":["Shabalin I.G.","Polyakov K.M.","Skirgello O.E.","Tishkov V.I.","Popov V.O."]}}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsSite: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

250835

PDB entries from 2026-03-18

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