Molecular docking of BBD-7, BBR-9, and vemurafenib against BRAF and CRAF.

<p><b>(A)</b> BBR-7/BRAF interactions; <b>(B)</b> Vemurafenib/BRAF interactions. Lys483 formed H-bonds (green lines) and Phe583 and Trp531 formed π-π interactions (purple lines); <b>(C, D, E)</b> Interactions of BBR-9 and neighboring residues of BRAF in binding cavity. Purple lines show T-shaped π-π interactions. BBR-9 indicates inter- and intra-molecular π-π interactions; <b>(F,G)</b> CRAF/BBR-9 docking; <b>(F)</b> Neighboring residues in the CRAF binding cavity; <b>(G)</b> Results from docking showing the different residues involved in CRAF/BBR-9 interactions. Lys375, Asp486, Phe475, Ser359, and Trp423 are the most important residues in CRAF docking; <b>(H)</b> The average energies of docking of BBR-9 and two controls, vemurafenib and ATP.