5DN9
Crystal structure of Candida boidinii formate dehydrogenase 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 | 0005739 | cellular_component | mitochondrion |
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 | 0005739 | cellular_component | mitochondrion |
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 | 37 |
Details | binding site for residue NAD A 501 |
Chain | Residue |
A | PHE69 |
A | TYR194 |
A | ASP195 |
A | TYR196 |
A | ALA229 |
A | PRO230 |
A | HIS232 |
A | THR235 |
A | THR256 |
A | ALA257 |
A | ARG258 |
A | VAL93 |
A | ASP282 |
A | VAL283 |
A | HIS311 |
A | SER313 |
A | GLY314 |
A | ALA357 |
A | AZI502 |
A | CL503 |
A | HOH668 |
A | HOH671 |
A | ASN119 |
A | HOH688 |
A | HOH702 |
A | HOH713 |
A | HOH735 |
A | HOH752 |
A | HOH799 |
A | HOH866 |
A | HOH932 |
A | VAL120 |
A | VAL123 |
A | GLY171 |
A | GLY173 |
A | ARG174 |
A | ILE175 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue AZI A 502 |
Chain | Residue |
A | PRO68 |
A | PHE69 |
A | GLY92 |
A | VAL93 |
A | ASN119 |
A | ARG258 |
A | HIS311 |
A | NAD501 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue CL A 503 |
Chain | Residue |
A | HIS232 |
A | NAD501 |
A | HOH1016 |
A | HOH1058 |
site_id | AC4 |
Number of Residues | 37 |
Details | binding site for residue NAD B 501 |
Chain | Residue |
B | PHE69 |
B | VAL93 |
B | ASN119 |
B | VAL120 |
B | VAL123 |
B | GLY171 |
B | GLY173 |
B | ARG174 |
B | ILE175 |
B | TYR194 |
B | ASP195 |
B | TYR196 |
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 | HOH675 |
B | HOH684 |
B | HOH685 |
B | HOH690 |
B | HOH706 |
B | HOH759 |
B | HOH772 |
B | HOH789 |
B | HOH874 |
B | HOH950 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue AZI B 502 |
Chain | Residue |
B | PRO68 |
B | PHE69 |
B | GLY92 |
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 | HOH1032 |
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 |