6JUK
Crystal structure of Formate dehydrogenase mutant C256I/E261P/S381I from Pseudomonas sp. 101 in complex with non-natural cofactor Nicotinamide Cytosine Dinucleotide
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 | 3 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | HIS30 |
| A | GLY33 |
| A | HOH608 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | TYR9 |
| A | ASP10 |
| A | TRP100 |
| A | HOH666 |
| A | HOH737 |
| B | TRP178 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | THR74 |
| A | SER75 |
| A | HOH724 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 504 |
| Chain | Residue |
| A | TYR20 |
| A | ARG22 |
| A | ASP23 |
| A | THR46 |
| A | PRO47 |
| A | GLY48 |
| B | HOH627 |
| site_id | AC5 |
| Number of Residues | 25 |
| Details | binding site for residue A7R A 505 |
| Chain | Residue |
| A | PHE99 |
| A | ASN147 |
| A | VAL151 |
| A | ALA199 |
| A | GLY201 |
| A | ARG202 |
| A | ILE203 |
| A | ASP222 |
| A | ARG223 |
| A | ASN255 |
| A | ILE256 |
| A | PRO257 |
| A | HIS259 |
| A | THR283 |
| A | ALA284 |
| A | ASP309 |
| A | HIS333 |
| A | SER335 |
| A | GLY336 |
| A | HOH624 |
| A | HOH663 |
| A | HOH707 |
| A | HOH741 |
| A | HOH771 |
| A | HOH773 |
| site_id | AC6 |
| Number of Residues | 23 |
| Details | binding site for residue A7R B 501 |
| Chain | Residue |
| B | PHE99 |
| B | ASN147 |
| B | VAL151 |
| B | ALA199 |
| B | GLY201 |
| B | ARG202 |
| B | ILE203 |
| B | ASP222 |
| B | ARG223 |
| B | ASN255 |
| B | ILE256 |
| B | PRO257 |
| B | HIS259 |
| B | THR283 |
| B | ALA284 |
| B | ASP309 |
| B | HIS333 |
| B | SER335 |
| B | GLY336 |
| B | HOH606 |
| B | HOH645 |
| B | HOH682 |
| B | HOH740 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | ARG360 |
| B | PRO361 |
| site_id | AC8 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | HIS259 |
| B | HOH615 |
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 site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"2006","firstPage":"627","lastPage":"631","volume":"51","journal":"Crystallogr. Rep.","title":"Crystal structure of the complex of NAD-dependent formate dehydrogenase from methylotrophic bacterium Pseudomonas sp.101 with formate.","authors":["Filippova E.V.","Polyakov K.M.","Tikhonova T.V.","Stekhanova T.N.","Boiko K.M.","Sadihov I.G.","Tishkov V.I.","Labrou N.","Popov V.O."],"citationCrossReferences":[{"database":"DOI","id":"10.1134/S1063774506040146"}]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8114093","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8114093","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
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 |
