8J83
Crystal structure of formate dehydrogenase from Methylorubrum extorquens AM1
Summary for 8J83
| Entry DOI | 10.2210/pdb8j83/pdb |
| Descriptor | Tungsten-containing formate dehydrogenase alpha subunit, Tungsten-containing formate dehydrogenase beta subunit, 2-AMINO-5,6-DIMERCAPTO-7-METHYL-3,7,8A,9-TETRAHYDRO-8-OXA-1,3,9,10-TETRAAZA-ANTHRACEN-4-ONE GUANOSINE DINUCLEOTIDE, ... (10 entities in total) |
| Functional Keywords | oxidoreductase, formate dehydrogenase, nad+ dependent, tungsten-containing, metallopterin guanine dinucleotide |
| Biological source | Methylorubrum extorquens AM1 More |
| Total number of polymer chains | 2 |
| Total formula weight | 174307.60 |
| Authors | Kobayashi, A.,Taketa, M.,Sowa, K.,Kano, K.,Higuchi, Y.,Ogata, H. (deposition date: 2023-04-29, release date: 2023-10-11) |
| Primary citation | Kobayashi, A.,Taketa, M.,Sowa, K.,Kano, K.,Higuchi, Y.,Ogata, H. Structure and function relationship of formate dehydrogenases: an overview of recent progress. Iucrj, 10:544-554, 2023 Cited by PubMed Abstract: Formate dehydrogenases (FDHs) catalyze the two-electron oxidation of formate to carbon dioxide. FDHs can be divided into several groups depending on their subunit composition and active-site metal ions. Metal-dependent (Mo- or W-containing) FDHs from prokaryotic organisms belong to the superfamily of molybdenum enzymes and are members of the dimethylsulfoxide reductase family. In this short review, recent progress in the structural analysis of FDHs together with their potential biotechnological applications are summarized. PubMed: 37668215DOI: 10.1107/S2052252523006437 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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