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6D4B

Crystal structure of Candida boidinii formate dehydrogenase V123A mutant complexed with NAD+ and azide

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0008863molecular_functionformate dehydrogenase (NAD+) activity
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0019752biological_processcarboxylic acid metabolic process
A0042183biological_processformate catabolic process
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005829cellular_componentcytosol
B0008863molecular_functionformate dehydrogenase (NAD+) activity
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0019752biological_processcarboxylic acid metabolic process
B0042183biological_processformate catabolic process
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues35
Detailsbinding site for residue NAD A 501
ChainResidue
APHE69
AASP195
ATYR196
AALA229
APRO230
AHIS232
ATHR235
ATHR256
AALA257
AARG258
AASP282
AVAL93
AVAL283
AHIS311
ASER313
AGLY314
AALA357
AAZI502
ACL503
AHOH644
AHOH683
AHOH696
AASN119
AHOH739
AHOH746
AHOH751
AHOH754
AHOH757
AHOH897
AVAL120
AGLY171
AGLY173
AARG174
AILE175
ATYR194

site_idAC2
Number of Residues7
Detailsbinding site for residue AZI A 502
ChainResidue
APRO68
APHE69
AVAL93
AASN119
AARG258
AHIS311
ANAD501

site_idAC3
Number of Residues3
Detailsbinding site for residue CL A 503
ChainResidue
AHIS232
ANAD501
AHOH1069

site_idAC4
Number of Residues36
Detailsbinding site for residue NAD B 501
ChainResidue
BPHE69
BVAL93
BASN119
BVAL120
BGLY171
BGLY173
BARG174
BILE175
BTYR194
BASP195
BTYR196
BASN228
BALA229
BPRO230
BHIS232
BTHR235
BTHR256
BALA257
BARG258
BASP282
BVAL283
BHIS311
BSER313
BGLY314
BALA357
BAZI502
BCL503
BHOH667
BHOH693
BHOH700
BHOH704
BHOH747
BHOH794
BHOH808
BHOH822
BHOH831

site_idAC5
Number of Residues7
Detailsbinding site for residue AZI B 502
ChainResidue
BPRO68
BPHE69
BVAL93
BASN119
BARG258
BHIS311
BNAD501

site_idAC6
Number of Residues3
Detailsbinding site for residue CL B 503
ChainResidue
BHIS232
BNAD501
BHOH1037

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues29
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IATIGaGRIGyrvlerlvpfnpkeLLyYD
ChainResidueDetails
AILE167-ASP195

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LVaqADIVtINaPlhagTkgLiN
ChainResidueDetails
ALEU218-ASN240

site_idPS00671
Number of Residues17
DetailsD_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. FKkGaWLVNtARGaICV
ChainResidueDetails
APHE247-VAL263

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PDB entries from 2024-05-01

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