1dld | pdb_00001dld

KNOWLEDGE-BASED MODELING OF THE D-LACTATE DEHYDROGENASE THREE-DIMENSIONAL STRUCTURE

spinqualitylabelsall models 1dld Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, PDBsum Publication Abstract from PubMed A three-dimensional structure of the NAD-dependent D-lactate dehydrogenase of Lactobacillus bulgaricus is modeled using the structure of the formate dehydrogenase of Pseudomonas sp. as template. Both sequences share only 22% of identical residues. Regions for knowledge-based modeling are defined from the structurally conserved regions predicted by multiple alignment of a set of related protein sequences with low homology. The model of the D-LDH subunit shows, as for the formate dehydrogenase, an alpha/beta structure, with a catalytic domain and a coenzyme binding domain. It points out the catalytic histidine (His-296) and supports the hypothetical catalytic mechanism. It also suggests that the other residues involved in the active site are Arg-235, possibly involved in the binding of the carboxyl group of the pyruvate, and Phe-299, a candidate for stabilizing the methyl group of the substrate. Knowledge-based modeling of the D-lactate dehydrogenase three-dimensional structure.,Vinals C, De Bolle X, Depiereux E, Feytmans E Proteins. 1995 Apr;21(4):307-18. PMID:7567953 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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