6JWG
Crystal structure of Formate dehydrogenase mutant C256I/E261P/S381I from Pseudomonas sp. 101
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 | 0032787 | biological_process | monocarboxylic acid metabolic process |
| 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 | 0032787 | biological_process | monocarboxylic acid metabolic process |
| 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
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|DOI:10.1134/S1063774506040146 |
| Chain | Residue | Details |
| A | ILE123 | |
| A | ASN147 | |
| B | ILE123 | |
| B | ASN147 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000269|PubMed:8114093 |
| 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 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | SITE: Important for catalytic activity => ECO:0000255|HAMAP-Rule:MF_03210, ECO:0000305|PubMed:8114093 |
| 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 |
