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. Author manuscript; available in PMC: 2012 Aug 30.
Published in final edited form as: Biochemistry. 2011 Aug 8;50(34):7426–7439. doi: 10.1021/bi2006866

Figure 7.

Figure 7

Stereo views of hedKR in silico docking analyses. HedKR monomer A is portrayed in teal in each panel. (A) Quercetin (blue) docking. A quercetin hydroxyl group is within hydrogen-bonding distance of the catalytic S142 and Y155 sidechains, as well as within hydride-transfer distance from C4 of the NADPH nicotinamide moiety. The residues modeled as sticks are targets for site-directed mutagenesis studies to determine long-ranged substrate pocket motifs that affect hedKR stereospecificity. (B) Three examples of emodin docked in hedKR (green, pink and yellow), overlaid with the emodin molecules from the previously solved P94L actKR cocrystal structure (white). The hedKR-emodin docking solutions were not consistent and do not overlap with the emodins in the actKR crystal structures. (C) S-tetralol (green) and R-tetralol (magenta) docked within the hedKR active site. The rigid benzene ring of R-tetralol is sterically hindered by the N92 sidechain that juts into the pocket.