1H0H
Tungsten containing Formate Dehydrogenase from Desulfovibrio Gigas
Summary for 1H0H
| Entry DOI | 10.2210/pdb1h0h/pdb |
| Descriptor | FORMATE DEHYDROGENASE SUBUNIT ALPHA, FORMATE DEHYDROGENASE SUBUNIT BETA, TUNGSTEN ION, ... (10 entities in total) |
| Functional Keywords | electron transport, tungsten selenium formate dehydrogenase, selenocysteine, molybdopterin, mgd, iron-sulphur cluster, periplasmic |
| Biological source | DESULFOVIBRIO GIGAS More |
| Total number of polymer chains | 4 |
| Total formula weight | 274267.64 |
| Authors | Raaijmakers, H.C.A. (deposition date: 2002-06-19, release date: 2003-02-20, Last modification date: 2024-10-23) |
| Primary citation | Raaijmakers, H.C.A.,Macieira, S.,Dias, J.,Teixeira, S.,Bursakov, S.,Huber, R.,Moura, J.,Moura, I.,Romao, M. Gene Sequence and the 1.8 A Crystal Structure of the Tungsten-Containing Formate Dehydrogenase from Desulfovibrio Gigas Structure, 10:1261-, 2002 Cited by PubMed Abstract: Desulfovibrio gigas formate dehydrogenase is the first representative of a tungsten-containing enzyme from a mesophile that has been structurally characterized. It is a heterodimer of 110 and 24 kDa subunits. The large subunit, homologous to E. coli FDH-H and to D. desulfuricans nitrate reductase, harbors the W site and one [4Fe-4S] center. No small subunit ortholog containing three [4Fe-4S] clusters has been reported. The structural homology with E. coli FDH-H shows that the essential residues (SeCys158, His159, and Arg407) at the active site are conserved. The active site is accessible via a positively charged tunnel, while product release may be facilitated, for H(+) by buried waters and protonable amino acids and for CO(2) through a hydrophobic channel. PubMed: 12220497DOI: 10.1016/S0969-2126(02)00826-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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