3WR5
Structural basis on the efficient CO2 reduction of acidophilic formate dehydrogenase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0008863 | molecular_function | formate dehydrogenase (NAD+) 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 | 0005737 | cellular_component | cytoplasm |
| B | 0008863 | molecular_function | formate dehydrogenase (NAD+) 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 |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| C | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| C | 0042183 | biological_process | formate catabolic process |
| C | 0051287 | molecular_function | NAD binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| D | 0016616 | molecular_function | oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor |
| D | 0042183 | biological_process | formate catabolic process |
| D | 0051287 | molecular_function | NAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD A 501 |
| Chain | Residue |
| A | PHE99 |
| A | ASP222 |
| A | ARG223 |
| A | HIS224 |
| A | ASN255 |
| A | VAL256 |
| A | PRO257 |
| A | HIS259 |
| A | GLU261 |
| A | THR262 |
| A | THR283 |
| A | ILE123 |
| A | ARG285 |
| A | ASP309 |
| A | VAL310 |
| A | HIS333 |
| A | SER335 |
| A | GLY336 |
| A | SER381 |
| A | HOH610 |
| A | HOH614 |
| A | HOH616 |
| A | ASN147 |
| A | HOH620 |
| A | HOH629 |
| A | HOH682 |
| A | HOH915 |
| A | HOH916 |
| A | SER148 |
| A | VAL151 |
| A | ALA199 |
| A | GLY201 |
| A | ARG202 |
| A | ILE203 |
| site_id | AC2 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD B 501 |
| Chain | Residue |
| B | ILE123 |
| B | ASN147 |
| B | SER148 |
| B | VAL151 |
| B | ALA199 |
| B | GLY201 |
| B | ARG202 |
| B | ILE203 |
| B | ASP222 |
| B | ARG223 |
| B | HIS224 |
| B | ASN255 |
| B | VAL256 |
| B | PRO257 |
| B | HIS259 |
| B | GLU261 |
| B | THR262 |
| B | THR283 |
| B | ALA284 |
| B | ARG285 |
| B | ASP309 |
| B | HIS333 |
| B | SER335 |
| B | GLY336 |
| B | SER381 |
| B | HOH609 |
| B | HOH610 |
| B | HOH613 |
| B | HOH664 |
| B | HOH666 |
| B | HOH705 |
| B | HOH753 |
| B | HOH808 |
| B | HOH810 |
| B | HOH884 |
| site_id | AC3 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE NAD C 501 |
| Chain | Residue |
| C | HOH658 |
| C | HOH666 |
| C | HOH672 |
| C | HOH692 |
| C | ILE123 |
| C | ASN147 |
| C | SER148 |
| C | VAL151 |
| C | ALA199 |
| C | GLY201 |
| C | ARG202 |
| C | ILE203 |
| C | ASP222 |
| C | ARG223 |
| C | HIS224 |
| C | ASN255 |
| C | VAL256 |
| C | PRO257 |
| C | HIS259 |
| C | GLU261 |
| C | THR262 |
| C | THR283 |
| C | ALA284 |
| C | ARG285 |
| C | ASP309 |
| C | VAL310 |
| C | HIS333 |
| C | SER335 |
| C | GLY336 |
| C | SER381 |
| C | HOH625 |
| C | HOH626 |
| C | HOH631 |
| C | HOH643 |
Functional Information from PROSITE/UniProt
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MYphCDVVtLNvPlhpeTehMiN |
| Chain | Residue | Details |
| A | MET245-ASN267 |
