4XYB
GRANULICELLA M. FORMATE DEHYDROGENASE (FDH) IN COMPLEX WITH NADP(+) AND NaN3
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005737 | cellular_component | cytoplasm |
| 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 | 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 NDP A 401 |
| Chain | Residue |
| A | PHE99 |
| A | ARG223 |
| A | HIS224 |
| A | HIS255 |
| A | PRO257 |
| A | TYR259 |
| A | THR262 |
| A | THR283 |
| A | ALA284 |
| A | ARG285 |
| A | ASP309 |
| A | ILE123 |
| A | HIS333 |
| A | SER335 |
| A | GLY336 |
| A | SER381 |
| A | TYR382 |
| A | AZI402 |
| A | HOH537 |
| A | HOH628 |
| A | HOH632 |
| A | HOH638 |
| A | ASN147 |
| A | HOH650 |
| A | HOH656 |
| A | HOH670 |
| A | HOH674 |
| A | HOH679 |
| A | HOH682 |
| A | HOH736 |
| A | HOH774 |
| A | VAL151 |
| A | ALA199 |
| A | GLY201 |
| A | ARG202 |
| A | ILE203 |
| A | ALA222 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | binding site for residue AZI A 402 |
| Chain | Residue |
| A | PRO98 |
| A | PHE99 |
| A | GLY122 |
| A | ILE123 |
| A | ASN147 |
| A | ARG285 |
| A | HIS333 |
| A | NDP401 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue EDO A 403 |
| Chain | Residue |
| A | ARG22 |
| A | ASN23 |
| A | GLY48 |
| B | HOH666 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | binding site for residue EDO A 404 |
| Chain | Residue |
| A | ASN39 |
| A | GLU351 |
| A | GLU354 |
| A | CYS355 |
| A | ARG360 |
| A | HOH520 |
| A | HOH550 |
| B | ARG30 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 405 |
| Chain | Residue |
| A | ARG225 |
| A | HOH529 |
| A | HOH558 |
| B | PRO317 |
| B | ALA318 |
| site_id | AC6 |
| Number of Residues | 38 |
| Details | binding site for residue NDP B 401 |
| Chain | Residue |
| B | HOH969 |
| B | PHE99 |
| B | ILE123 |
| B | ASN147 |
| B | VAL151 |
| B | ALA199 |
| B | GLY201 |
| B | ARG202 |
| B | ILE203 |
| B | ALA222 |
| B | ARG223 |
| B | HIS224 |
| B | HIS255 |
| B | PRO257 |
| B | TYR259 |
| B | THR262 |
| B | THR283 |
| B | ALA284 |
| B | ARG285 |
| B | ASP309 |
| B | HIS333 |
| B | SER335 |
| B | GLY336 |
| B | SER381 |
| B | TYR382 |
| B | AZI402 |
| B | HOH639 |
| B | HOH646 |
| B | HOH651 |
| B | HOH656 |
| B | HOH667 |
| B | HOH672 |
| B | HOH715 |
| B | HOH811 |
| B | HOH814 |
| B | HOH817 |
| B | HOH856 |
| B | HOH871 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue AZI B 402 |
| Chain | Residue |
| B | PRO98 |
| B | PHE99 |
| B | GLY122 |
| B | ILE123 |
| B | ASN147 |
| B | ARG285 |
| B | HIS333 |
| B | NDP401 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | binding site for residue EDO B 403 |
| Chain | Residue |
| A | ARG30 |
| B | ASN39 |
| B | GLU351 |
| B | GLU354 |
| B | CYS355 |
| B | ARG360 |
| B | HOH521 |
| B | HOH535 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | binding site for residue EDO B 404 |
| Chain | Residue |
| B | HIS170 |
| B | GLU174 |
| B | HOH851 |
