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homology modeling of structure. The substrate binding pocket consists of residues P122, W123, E125, S174, N179, V180, S214, P215, G217, Y218, I223, S224, D225, F226 and V227, with all of the residues lying in the flexible loop regions
apo-enzyme and bound to NAD+, at a resolution of 2.1 and 2.4 A, respectively. Enzyme is a tetamer with two types of hydrophobic interfaces. NAD+-binding is associated with a conformational shift of the substrate binding loop from a crystallographically unordered open to a more ordered closed form