Functional Information from GO Data
Chain | GOid | namespace | contents |
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 | 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 | 6 |
Details | binding site for residue GOL A 501 |
Chain | Residue |
A | ARG22 |
A | ASP23 |
A | PRO47 |
A | GLY48 |
A | HOH862 |
B | HOH623 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue TRS A 502 |
Chain | Residue |
A | HOH820 |
A | ARG202 |
A | ILE203 |
A | HOH819 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue GOL B 501 |
Chain | Residue |
B | GLY201 |
B | ARG202 |
B | ILE203 |
B | HOH682 |
Functional Information from PROSITE/UniProt
site_id | PS00065 |
Number of Residues | 28 |
Details | D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. VGTVAaGRIGlavlrrlapfdvh.LHyTD |
Chain | Residue | Details |
A | VAL195-ASP222 | |
site_id | PS00670 |
Number of Residues | 23 |
Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MYpvCDVVtLNiPlhppTehMiN |
Chain | Residue | Details |
A | MET245-ASN267 | |
site_id | PS00671 |
Number of Residues | 17 |
Details | D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. FKrGaYIVNtARGkLCD |
Chain | Residue | Details |
A | PHE274-ASP290 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ILE123 | |
A | ASN147 | |
B | ILE123 | |
B | ASN147 | |
Chain | Residue | Details |
A | SER148 | |
B | ARG202 | |
B | ASP222 | |
B | PRO257 | |
B | THR283 | |
B | ASP309 | |
B | HIS333 | |
B | ILE381 | |
A | ARG202 | |
A | ASP222 | |
A | PRO257 | |
A | THR283 | |
A | ASP309 | |
A | HIS333 | |
A | ILE381 | |
B | SER148 | |
Chain | Residue | Details |
A | ARG285 | |
A | HIS333 | |
B | ARG285 | |
B | HIS333 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 902 |
Chain | Residue | Details |
A | ASN147 | electrostatic stabiliser |
A | ARG285 | electrostatic stabiliser |
A | GLN314 | modifies pKa |
A | HIS333 | enhance reactivity |
site_id | MCSA2 |
Number of Residues | 4 |
Details | M-CSA 902 |
Chain | Residue | Details |
B | ASN147 | electrostatic stabiliser |
B | ARG285 | electrostatic stabiliser |
B | GLN314 | modifies pKa |
B | HIS333 | enhance reactivity |