3JTM
Structure of recombinant formate dehydrogenase from Arabidopsis thaliana
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005829 | cellular_component | cytosol |
| A | 0008863 | molecular_function | formate dehydrogenase (NAD+) activity |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009536 | cellular_component | plastid |
| A | 0009579 | cellular_component | thylakoid |
| A | 0009611 | biological_process | response to wounding |
| 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1 |
| Chain | Residue |
| A | ARG354 |
| A | PRO362 |
| A | HOH432 |
| A | HOH580 |
| A | HOH590 |
| A | HOH671 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 3 |
| Chain | Residue |
| A | LYS45 |
| A | TYR184 |
| A | ARG185 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 4 |
| Chain | Residue |
| A | TYR102 |
| A | THR104 |
| A | LYS204 |
| A | LEU223 |
| A | MET225 |
| A | ALA226 |
| A | LEU229 |
| A | HOH459 |
| A | HOH635 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 5 |
| Chain | Residue |
| A | HOH7 |
| A | VAL53 |
| A | GLU54 |
| A | ASN55 |
| A | ALA56 |
| A | ARG60 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL A 8 |
| Chain | Residue |
| A | PRO97 |
| A | PHE98 |
| A | GLY121 |
| A | ILE122 |
| A | ASN146 |
| A | GLY335 |
| A | TYR344 |
| A | HOH400 |
| A | HOH403 |
| A | HOH622 |
| A | HOH756 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 9 |
| Chain | Residue |
| A | LEU57 |
| A | GLY58 |
| A | LYS349 |
| A | GOL386 |
| A | HOH437 |
| A | HOH475 |
| A | HOH484 |
| A | HOH492 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 11 |
| Chain | Residue |
| A | ASN146 |
| A | ASN282 |
| A | ALA283 |
| A | HOH440 |
| A | HOH622 |
| A | HOH717 |
| site_id | AC8 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE AZI A 379 |
| Chain | Residue |
| A | ASP360 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 380 |
| Chain | Residue |
| A | ARG290 |
| A | PRO312 |
| A | PRO316 |
| A | ASP318 |
| site_id | BC1 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 381 |
| Chain | Residue |
| A | TYR187 |
| A | ASP249 |
| site_id | BC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 382 |
| Chain | Residue |
| A | ILE108 |
| A | LYS109 |
| A | ALA111 |
| A | LYS112 |
| A | THR363 |
| A | GLN376 |
| A | HOH505 |
| A | HOH662 |
| A | HOH747 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 383 |
| Chain | Residue |
| A | GLY123 |
| A | SER124 |
| A | ASP125 |
| A | GLU141 |
| A | ILE367 |
| A | TYR377 |
| A | HOH586 |
| site_id | BC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 384 |
| Chain | Residue |
| A | GLY200 |
| A | ARG201 |
| A | GOL387 |
| site_id | BC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AZI A 385 |
| Chain | Residue |
| A | LEU161 |
| A | ASN164 |
| A | GLY303 |
| A | GLY304 |
| A | ASN326 |
| A | HOH596 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 386 |
| Chain | Residue |
| A | GOL9 |
| A | LYS349 |
| A | HOH435 |
| site_id | BC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 387 |
| Chain | Residue |
| A | THR104 |
| A | ALA105 |
| A | GLU106 |
| A | ASP128 |
| A | GLY200 |
| A | ASP221 |
| A | GOL384 |
| A | HOH434 |
| A | HOH742 |
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. IGTVGaGRIGklllqrlkpfgcn.LLyHD |
| Chain | Residue | Details |
| A | ILE194-ASP221 |
| site_id | PS00670 |
| Number of Residues | 23 |
| Details | D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. MLpkCDVIvINmPltekTrgMfN |
| 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. LKkGvLIVNnARGaIME |
| Chain | Residue | Details |
| A | LEU273-GLU289 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 11 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"MAY-2010","submissionDatabase":"PDB data bank","title":"Structures of the apo and holo forms of NAD-dependent formate dehydrogenase from the higher-plant Arabidopsis thaliana.","authors":["Shabalin I.G.","Polyakov K.M.","Skirgello O.E.","Tishkov V.I.","Popov V.O."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"HAMAP-Rule","id":"MF_03210","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
