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. Author manuscript; available in PMC: 2018 Jun 20.
Published in final edited form as: Biochemistry. 2017 Jun 7;56(24):3058–3067. doi: 10.1021/acs.biochem.7b00334

Figure 9.

Figure 9

Crystal structure of the RIT-bound Cys-less CYP3A4. (A) Superposition of RIT-bound Cys-less (beige and orange) and WT CYP3A4 (green) shows conformational differences in the F–G fragment and C-terminal loop. (B) RIT orientation in Cys-less (magenta) and WT CYP3A4 (yellow). In the mutant, the disordered isopropyl thiazole portion of RIT is depicted in thin lines. The C58A substitution triggers repositioning of the Phe57 and Met371 side chains, due to which the RIT terminal group and the F′–G′ loop (residues 211–217) accommodate distinct conformations to avoid steric clashing. The 2Fo – Fc and simulated annealing Fo – Fc omit maps around RIT in Cys-less CYP3A4 are shown as gray and green mesh contoured at 1σ and 3σ, respectively.