Studies on 16α-Hydroxylation of Steroid Molecules and Regioselective Binding Mode in Homology-Modeled Cytochrome P450-2C11
Figure 3
Docking configurations of inhibitors 32 and 33 (yellow ball and stick) into the homology-modeled CYP2C11 where amino acid residues G296, A297, and L366 are hidden for clarity. (a) The relevant amino acid (wire, colored by atoms) biding sites with the inhibitors are shown, and both inhibitors are docked in a superimposed fashion with the embedded substrate flurbiprofen (FLP, wire in blue) within RMSD of 0.93 and 0.79 Å, respectively. (b) Inhibitor 32 exhibits the planar A-B ring binding configuration with heme molecule (stick in red), while inhibitor 33, the bent A-B ring binding configuration. The distance between C16-carbon of inhibitor 32 and the heme iron is 5.26 Å with the angle between C16 carbon, C16- hydrogen, and the heme iron being 160.9°, while the formaer of inhibitor 33, 5.70 Å, and the latter, 150.6°.
