6D4B
Crystal structure of Candida boidinii formate dehydrogenase V123A mutant complexed with NAD+ and azide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| 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 | 0042183 | biological_process | formate catabolic process |
| A | 0051287 | molecular_function | NAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| 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 | 0042183 | biological_process | formate catabolic process |
| B | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 35 |
| Details | binding site for residue NAD A 501 |
| Chain | Residue |
| A | PHE69 |
| A | ASP195 |
| A | TYR196 |
| A | ALA229 |
| A | PRO230 |
| A | HIS232 |
| A | THR235 |
| A | THR256 |
| A | ALA257 |
| A | ARG258 |
| A | ASP282 |
| A | VAL93 |
| A | VAL283 |
| A | HIS311 |
| A | SER313 |
| A | GLY314 |
| A | ALA357 |
| A | AZI502 |
| A | CL503 |
| A | HOH644 |
| A | HOH683 |
| A | HOH696 |
| A | ASN119 |
| A | HOH739 |
| A | HOH746 |
| A | HOH751 |
| A | HOH754 |
| A | HOH757 |
| A | HOH897 |
| A | VAL120 |
| A | GLY171 |
| A | GLY173 |
| A | ARG174 |
| A | ILE175 |
| A | TYR194 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue AZI A 502 |
| Chain | Residue |
| A | PRO68 |
| A | PHE69 |
| A | VAL93 |
| A | ASN119 |
| A | ARG258 |
| A | HIS311 |
| A | NAD501 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue CL A 503 |
| Chain | Residue |
| A | HIS232 |
| A | NAD501 |
| A | HOH1069 |
| site_id | AC4 |
| Number of Residues | 36 |
| Details | binding site for residue NAD B 501 |
| Chain | Residue |
| B | PHE69 |
| B | VAL93 |
| B | ASN119 |
| B | VAL120 |
| B | GLY171 |
| B | GLY173 |
| B | ARG174 |
| B | ILE175 |
| B | TYR194 |
| B | ASP195 |
| B | TYR196 |
| B | ASN228 |
| B | ALA229 |
| B | PRO230 |
| B | HIS232 |
| B | THR235 |
| B | THR256 |
| B | ALA257 |
| B | ARG258 |
| B | ASP282 |
| B | VAL283 |
| B | HIS311 |
| B | SER313 |
| B | GLY314 |
| B | ALA357 |
| B | AZI502 |
| B | CL503 |
| B | HOH667 |
| B | HOH693 |
| B | HOH700 |
| B | HOH704 |
| B | HOH747 |
| B | HOH794 |
| B | HOH808 |
| B | HOH822 |
| B | HOH831 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue AZI B 502 |
| Chain | Residue |
| B | PRO68 |
| B | PHE69 |
| B | VAL93 |
| B | ASN119 |
| B | ARG258 |
| B | HIS311 |
| B | NAD501 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue CL B 503 |
| Chain | Residue |
| B | HIS232 |
| B | NAD501 |
| B | HOH1037 |
Functional Information from PROSITE/UniProt
| site_id | PS00065 |
| Number of Residues | 29 |
| Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. IATIGaGRIGyrvlerlvpfnpkeLLyYD |
| Chain | Residue | Details |
| A | ILE167-ASP195 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LVaqADIVtINaPlhagTkgLiN |
| Chain | Residue | Details |
| A | LEU218-ASN240 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. FKkGaWLVNtARGaICV |
| Chain | Residue | Details |
| A | PHE247-VAL263 |
