X-ray crystal structure of the cytochrome P450 2B4 active site mutant F297A in complex with clopidogrel: Insights into compensatory rearrangements of the binding pocket

► The crystal structure of a P450 2B4 F297A complex with clopidogrel was determined. ► The orientation of clopidogrel in the active site differed from the wild type. ► Movement of the I helix and other active site residues was also observed in F297A. ► A virtual F297A with the I helix repositioned is a reasonable template for docking. ► The orientation of F202 correlates with detergent binding in a peripheral pocket.