Figure 1.

X-ray crystal structure of 5 in complex with B-Raf^WT. The cleft surface is rendered in violet, select residues are depicted in white, and the inhibitor is green. Hydrogen-bonding interactions are illustrated with yellow dashed lines. Several residues that are involved in hydrophobic interactions with 5 are omitted for clarity and described in the text. The propyl group resides in a pocket that is enlarged by an outward shift of the αC-helix. The DFG sequence (D594-G596) resides in its active (DFG-in) conformation.