6T9X
Crystal structure of formate dehydrogenase FDH2 D222Q/Q223R mutant enzyme from Granulicella mallensis MP5ACTX8 in complex with NADP 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 | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| 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 | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| 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 | 0000166 | molecular_function | nucleotide binding |
| C | 0005737 | cellular_component | cytoplasm |
| C | 0005829 | cellular_component | cytosol |
| C | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| 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 | 0000166 | molecular_function | nucleotide binding |
| D | 0005737 | cellular_component | cytoplasm |
| D | 0005829 | cellular_component | cytosol |
| D | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016614 | molecular_function | oxidoreductase activity, acting on CH-OH group of donors |
| 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 | 7 |
| Details | binding site for residue AZI B 701 |
| Chain | Residue |
| B | PRO98 |
| B | PHE99 |
| B | ILE123 |
| B | ASN147 |
| B | ARG285 |
| B | HIS333 |
| B | NAP702 |
| site_id | AC2 |
| Number of Residues | 37 |
| Details | binding site for residue NAP B 702 |
| Chain | Residue |
| B | ASN147 |
| B | SER148 |
| B | VAL151 |
| B | ALA199 |
| B | GLY201 |
| B | ARG202 |
| B | ILE203 |
| B | PHE221 |
| B | GLN222 |
| B | ARG223 |
| B | HIS224 |
| B | ASN255 |
| B | ALA256 |
| B | PRO257 |
| B | HIS259 |
| B | THR262 |
| B | THR283 |
| B | ALA284 |
| B | ARG285 |
| B | ASP309 |
| B | HIS333 |
| B | SER335 |
| B | GLY336 |
| B | HIS380 |
| B | SER381 |
| B | TYR382 |
| B | AZI701 |
| B | HOH808 |
| B | HOH830 |
| B | HOH838 |
| B | HOH844 |
| B | HOH883 |
| B | HOH907 |
| B | HOH915 |
| B | HOH938 |
| B | PHE99 |
| B | ILE123 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue AZI A 701 |
| Chain | Residue |
| A | PRO98 |
| A | PHE99 |
| A | ILE123 |
| A | ASN147 |
| A | ARG285 |
| A | HIS333 |
| A | NAP702 |
| site_id | AC4 |
| Number of Residues | 37 |
| Details | binding site for residue NAP A 702 |
| Chain | Residue |
| A | PHE99 |
| A | ILE123 |
| A | ASN147 |
| A | SER148 |
| A | VAL151 |
| A | ALA199 |
| A | GLY201 |
| A | ARG202 |
| A | ILE203 |
| A | PHE221 |
| A | GLN222 |
| A | ARG223 |
| A | HIS224 |
| A | ASN255 |
| A | PRO257 |
| A | HIS259 |
| A | THR262 |
| A | THR283 |
| A | ALA284 |
| A | ARG285 |
| A | ASP309 |
| A | VAL310 |
| A | HIS333 |
| A | SER335 |
| A | GLY336 |
| A | HIS380 |
| A | SER381 |
| A | TYR382 |
| A | AZI701 |
| A | HOH820 |
| A | HOH833 |
| A | HOH853 |
| A | HOH859 |
| A | HOH866 |
| A | HOH868 |
| A | HOH887 |
| A | HOH901 |
| site_id | AC5 |
| Number of Residues | 7 |
| Details | binding site for residue AZI C 701 |
| Chain | Residue |
| C | PRO98 |
| C | PHE99 |
| C | ILE123 |
| C | ASN147 |
| C | ARG285 |
| C | HIS333 |
| C | NAP702 |
| site_id | AC6 |
| Number of Residues | 37 |
| Details | binding site for residue NAP C 702 |
| Chain | Residue |
| C | VAL151 |
| C | ALA199 |
| C | GLY201 |
| C | ARG202 |
| C | ILE203 |
| C | PHE221 |
| C | GLN222 |
| C | ARG223 |
| C | HIS224 |
| C | ASN255 |
| C | PRO257 |
| C | HIS259 |
| C | THR262 |
| C | THR283 |
| C | ALA284 |
| C | ARG285 |
| C | ASP309 |
| C | HIS333 |
| C | SER335 |
| C | GLY336 |
| C | HIS380 |
| C | SER381 |
| C | TYR382 |
| C | AZI701 |
| C | HOH808 |
| C | HOH813 |
| C | HOH837 |
| C | HOH867 |
| C | HOH877 |
| C | HOH900 |
| C | HOH929 |
| C | HOH951 |
| C | HOH969 |
| C | PHE99 |
| C | ILE123 |
| C | ASN147 |
| C | SER148 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue AZI D 701 |
| Chain | Residue |
| D | PRO98 |
| D | PHE99 |
| D | ILE123 |
| D | ASN147 |
| D | ARG285 |
| D | HIS333 |
| D | NAP702 |
| site_id | AC8 |
| Number of Residues | 37 |
| Details | binding site for residue NAP D 702 |
| Chain | Residue |
| D | PHE99 |
| D | ILE123 |
| D | ASN147 |
| D | SER148 |
| D | VAL151 |
| D | ALA199 |
| D | ALA200 |
| D | GLY201 |
| D | ARG202 |
| D | ILE203 |
| D | PHE221 |
| D | GLN222 |
| D | ARG223 |
| D | HIS224 |
| D | ASN255 |
| D | ALA256 |
| D | PRO257 |
| D | HIS259 |
| D | THR262 |
| D | THR283 |
| D | ALA284 |
| D | ARG285 |
| D | ASP309 |
| D | HIS333 |
| D | SER335 |
| D | GLY336 |
| D | HIS380 |
| D | SER381 |
| D | TYR382 |
| D | AZI701 |
| D | HOH814 |
| D | HOH838 |
| D | HOH840 |
| D | HOH843 |
| D | HOH888 |
| D | HOH912 |
| D | HOH922 |
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. MVkvCDVVtINaPlhpgTldLfN |
| Chain | Residue | Details |
| B | MET245-ASN267 |
| site_id | PS00671 |
| Number of Residues | 17 |
| Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. MKrGaYLVNtARGkICN |
| Chain | Residue | Details |
| B | MET274-ASN290 |
