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6T8C

Crystal structure of formate dehydrogenase FDH2 enzyme from Granulicella mallensis MP5ACTX8 in the apo form.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
A0008863molecular_functionformate dehydrogenase (NAD+) activity
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
B0000166molecular_functionnucleotide binding
B0005737cellular_componentcytoplasm
B0008863molecular_functionformate dehydrogenase (NAD+) activity
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
C0000166molecular_functionnucleotide binding
C0005737cellular_componentcytoplasm
C0008863molecular_functionformate dehydrogenase (NAD+) activity
C0016491molecular_functionoxidoreductase activity
C0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
C0032787biological_processmonocarboxylic acid metabolic process
C0042183biological_processformate catabolic process
C0051287molecular_functionNAD binding
D0000166molecular_functionnucleotide binding
D0005737cellular_componentcytoplasm
D0008863molecular_functionformate dehydrogenase (NAD+) activity
D0016491molecular_functionoxidoreductase activity
D0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
D0032787biological_processmonocarboxylic acid metabolic process
D0042183biological_processformate catabolic process
D0051287molecular_functionNAD binding
Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGTVAaGRIGlavlkrlkpfdvk.LHyFD
ChainResidueDetails
AVAL195-ASP222

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MVkvCDVVtINaPlhpgTldLfN
ChainResidueDetails
AMET245-ASN267

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKrGaYLVNtARGkICN
ChainResidueDetails
AMET274-ASN290

237735

PDB entries from 2025-06-18

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