Studies on 16α-Hydroxylation of Steroid Molecules and Regioselective Binding Mode in Homology-Modeled Cytochrome P450-2C11
Figure 4
The docking modes of different inhibitors, inh32, inh33, inh34, and inh56 (inhibitor code), are shown with ball and stick in yellow within the binding site pocket of Cyt P450-2C11. The embedded ligand, flurbiprofen (FLP, ball and stick colored by atoms) is bound inside the pocket of the homology-modeled Cyt P450-2C11. All inhibitors are docked within the distance of 4–6 Å (shown in lines and 3 digit numbers) between C16 and the iron atom of heme molecule (shown as red, stick) and with the angel between the 16C-hydrogen and the iron of heme molecule being 180 + 45° (shown in lines and 4 digit numbers). Pertinent amino acids (ASN107, ILE113, PHE114, ASN204 PHE205, PHE237 THR292, ASP293, GLY296, ALA297, GLU300, THR301, and LEU366) lay within 4 Å of all docked steroid molecules and are shown in stick, colored by atoms. Hydrogen bond formation is shown in dotted line between the inhibitor and amino the acid residue.
