NADH quinone oxidoreductase (NQO1) with inhibitor dicoumarol: Difference between revisions

The crystal structure of human NQO1 in complex with dicoumarol was determined at 2.75 Å resolution ([[2f1o]]). NQO1 is a <scene name='2f1o/Com_view/6'>physiological homodimer</scene> composed of two interlocked monomers. <scene name='2f1o/Com_view/7'>Two catalytic sites</scene> are formed and are present at the dimer interface (<font color='red'><b>FAD is colored red</b></font> and <font color='blue'><b>dicoumarol is colored blue</b></font>). Therefore, each from these two <scene name='2f1o/Active_site/3'>dicoumarol-hNQO1 binding sites</scene> is formed by both monomers. <font color='cyan'><b>Dicoumarol is colored cyan</b></font>, <font color='orange'><b>FAD in orange</b></font>, nitrogens and oxygens are shown in [http://en.wikipedia.org/wiki/CPK_coloring CPK colors]. NQO1 <font color='blueviolet'><b>chain A is colored blueviolet</b></font> and <font color='lime'><b>chain C in lime</b></font>.  NQO1 residues, participating in ligand interactions, are shown as stick representation and are labeled (A and C refer to the NQO1 chains). H-bonds are shown by dashed lines with their distances.