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 | 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 | 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 | 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 | 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 |