2NAD
HIGH RESOLUTION STRUCTURES OF HOLO AND APO FORMATE DEHYDROGENASE
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 | 8 |
| Details | BINDING SITE FOR RESIDUE AZI A 395 |
| Chain | Residue |
| A | PRO97 |
| A | PHE98 |
| A | GLY121 |
| A | ILE122 |
| A | ASN146 |
| A | ARG284 |
| A | HIS332 |
| A | NAD394 |
| site_id | AC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 396 |
| Chain | Residue |
| B | HIS263 |
| B | LYS286 |
| B | CYS288 |
| B | ASP289 |
| B | ARG290 |
| B | HOH448 |
| B | HOH675 |
| A | HOH523 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE AZI B 395 |
| Chain | Residue |
| B | PRO97 |
| B | PHE98 |
| B | ILE122 |
| B | ASN146 |
| B | ARG284 |
| B | HIS332 |
| B | NAD394 |
| site_id | AC4 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD A 394 |
| Chain | Residue |
| A | PHE98 |
| A | ILE122 |
| A | ASN146 |
| A | SER147 |
| A | VAL150 |
| A | ALA198 |
| A | GLY200 |
| A | ARG201 |
| A | ILE202 |
| A | ASP221 |
| A | ARG222 |
| A | HIS223 |
| A | ASN254 |
| A | PRO256 |
| A | HIS258 |
| A | GLU260 |
| A | THR261 |
| A | THR282 |
| A | ALA283 |
| A | ARG284 |
| A | ASP308 |
| A | VAL309 |
| A | HIS332 |
| A | SER334 |
| A | GLY335 |
| A | SER380 |
| A | TYR381 |
| A | AZI395 |
| A | HOH409 |
| A | HOH412 |
| A | HOH425 |
| A | HOH453 |
| A | HOH460 |
| A | HOH499 |
| A | HOH578 |
| site_id | AC5 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE NAD B 394 |
| Chain | Residue |
| B | PHE98 |
| B | ILE122 |
| B | ASN146 |
| B | SER147 |
| B | VAL150 |
| B | ALA198 |
| B | GLY200 |
| B | ARG201 |
| B | ILE202 |
| B | ASP221 |
| B | ARG222 |
| B | HIS223 |
| B | ASN254 |
| B | PRO256 |
| B | HIS258 |
| B | GLU260 |
| B | THR261 |
| B | THR282 |
| B | ALA283 |
| B | ARG284 |
| B | ASP308 |
| B | HIS332 |
| B | SER334 |
| B | GLY335 |
| B | SER380 |
| B | TYR381 |
| B | AZI395 |
| B | HOH397 |
| B | HOH398 |
| B | HOH399 |
| B | HOH400 |
| B | HOH426 |
| B | HOH436 |
| B | HOH495 |
| B | HOH575 |
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 | VAL194-ASP221 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MYpvCDVVtLNcPlhpeTehMiN |
| Chain | Residue | Details |
| A | MET244-ASN266 |
| 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 | PHE273-ASP289 |
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 | 26 |
| 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 | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 2nac |
| Chain | Residue | Details |
| A | GLN313 | |
| A | HIS332 | |
| A | ASN146 | |
| A | ARG284 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 2nac |
| Chain | Residue | Details |
| B | GLN313 | |
| B | HIS332 | |
| B | ASN146 | |
| B | ARG284 |
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 902 |
| Chain | Residue | Details |
| A | ASN146 | electrostatic stabiliser |
| A | ARG284 | electrostatic stabiliser |
| A | GLN313 | modifies pKa |
| A | HIS332 | enhance reactivity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 902 |
| Chain | Residue | Details |
| B | ASN146 | electrostatic stabiliser |
| B | ARG284 | electrostatic stabiliser |
| B | GLN313 | modifies pKa |
| B | HIS332 | enhance reactivity |
