6TTB
Crystal structure of NAD-dependent formate dehydrogenase from Staphylococcus aureus in complex with NAD
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0008720 | molecular_function | D-lactate dehydrogenase activity |
A | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
A | 0051287 | molecular_function | NAD binding |
B | 0000166 | molecular_function | nucleotide binding |
B | 0008720 | molecular_function | D-lactate dehydrogenase activity |
B | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 23 |
Details | binding site for residue NAD A 401 |
Chain | Residue |
A | PHE95 |
A | PRO219 |
A | HIS246 |
A | ALA247 |
A | PRO248 |
A | GLU252 |
A | THR253 |
A | THR274 |
A | ARG276 |
A | ASP300 |
A | HIS324 |
A | ASN143 |
A | SER326 |
A | GLY327 |
A | HOH502 |
A | HOH504 |
A | VAL147 |
A | PHE194 |
A | GLY197 |
A | ARG198 |
A | ILE199 |
A | TYR217 |
A | ASP218 |
Functional Information from PROSITE/UniProt
site_id | PS00065 |
Number of Residues | 28 |
Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IGIFGfGRIGqlvaerlapfnvt.LQhYD |
Chain | Residue | Details |
A | ILE191-ASP218 |
site_id | PS00670 |
Number of Residues | 23 |
Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LVssSDAItIHaPltpeTdnLfD |
Chain | Residue | Details |
A | LEU236-ASP258 |