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7ARZ

Ternary complex of NAD-dependent formate dehydrogenase from Physcomitrium patens

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005739cellular_componentmitochondrion
A0005829cellular_componentcytosol
A0008863molecular_functionformate dehydrogenase (NAD+) activity
A0009507cellular_componentchloroplast
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0042183biological_processformate catabolic process
A0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues29
Detailsbinding site for residue NAD A 501
ChainResidue
APHE121
AASN247
ATHR279
APRO280
AGLN284
AASN306
AALA307
AARG308
AASP332
AHIS356
ASER358
AASN169
AGLY359
AGLN400
ATYR401
AAZI502
AHOH617
AHOH627
AHOH631
AHOH651
AHOH653
AHOH660
AVAL170
AVAL173
AGLY223
AARG224
AILE225
AASP245
AARG246

site_idAC2
Number of Residues8
Detailsbinding site for residue AZI A 502
ChainResidue
APRO120
APHE121
AGLY144
AVAL145
AASN169
AARG308
AHIS356
ANAD501

site_idAC3
Number of Residues7
Detailsbinding site for residue AZI A 503
ChainResidue
ALEU116
ATHR118
ALEU140
AVAL141
ATHR142
AVAL162
ASER163

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues29
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGTVGgGRIGqelmkrlkgfglkeMLyYD
ChainResidueDetails
AVAL217-ASP245

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MLskCDVVvVNtPltdqTrgLfN
ChainResidueDetails
AMET268-ASN290

218853

PDB entries from 2024-04-24

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