1fdo

OXIDIZED FORM OF FORMATE DEHYDROGENASE H FROM E. COLIOXIDIZED FORM OF FORMATE DEHYDROGENASE H FROM E. COLI

Structural highlights 1fdo is a 1 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: , , Gene: FDHF ("Bacillus coli" Migula 1895) Activity: Formate dehydrogenase, with EC number 1.2.1.2 Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and an Fe4S4 cluster at the active site and catalyzes the two-electron oxidation of formate to carbon dioxide. The crystal structures of the oxidized [Mo(VI), Fe4S4(ox)] form of formate dehydrogenase H (with and without bound inhibitor) and the reduced [Mo(IV), Fe4S4(red)] form have been determined, revealing a four-domain alphabeta structure with the molybdenum directly coordinated to selenium and both MGD cofactors. These structures suggest a reaction mechanism that directly involves SeCys140 and His141 in proton abstraction and the molybdenum, molybdopterin, Lys44, and the Fe4S4 cluster in electron transfer. Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster.,Boyington JC, Gladyshev VN, Khangulov SV, Stadtman TC, Sun PD Science. 1997 Feb 28;275(5304):1305-8. PMID:9036855 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Formate dehydrogenase

spinqualitylabelsall models 1fdo, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image