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6TTB

Crystal structure of NAD-dependent formate dehydrogenase from Staphylococcus aureus in complex with NAD

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008720molecular_functionD-lactate dehydrogenase activity
A0008863molecular_functionformate dehydrogenase (NAD+) activity
A0016491molecular_functionoxidoreductase activity
A0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
A0051287molecular_functionNAD binding
B0000166molecular_functionnucleotide binding
B0008720molecular_functionD-lactate dehydrogenase activity
B0008863molecular_functionformate dehydrogenase (NAD+) activity
B0016491molecular_functionoxidoreductase activity
B0016616molecular_functionoxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
B0051287molecular_functionNAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues23
Detailsbinding site for residue NAD A 401
ChainResidue
APHE95
APRO219
AHIS246
AALA247
APRO248
AGLU252
ATHR253
ATHR274
AARG276
AASP300
AHIS324
AASN143
ASER326
AGLY327
AHOH502
AHOH504
AVAL147
APHE194
AGLY197
AARG198
AILE199
ATYR217
AASP218

Functional Information from PROSITE/UniProt
site_idPS00065
Number of Residues28
DetailsD_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IGIFGfGRIGqlvaerlapfnvt.LQhYD
ChainResidueDetails
AILE191-ASP218

site_idPS00670
Number of Residues23
DetailsD_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LVssSDAItIHaPltpeTdnLfD
ChainResidueDetails
ALEU236-ASP258

231029

PDB entries from 2025-02-05

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