Fig. 1

Results of docking studies. In color on the outside are amino acid residues while small molecules are represented with their chemical structure. H-bonds are represented as solid purple lines while pi-cation interactions are red. a Ligand interaction diagram between BV02 and SFN coordinated by H-bonds and pi-cation interaction. Several residues important for the protein-drug interaction include Lys-49, Arg-129, and Tyr-130. b Ligand interaction diagram between BV02 and YWHAZ involves different residues compared to SFN, e.g. Lys-49. c Figure legend for panels A, B, and E. d Free energy of binding (ΔG) for all seven 14–3-3 protein family member plotted for each small molecule inhibitors (BV02; BV02_9; COR: corannulene; DOC: docetaxel; ENZ: enzalutamide; MK2: MK2206). e Although docetaxel is only coordinated by a H-bond and a pi-cation interaction, the molecule fits squarely into the amphipathic binding groove resulting in very low ΔG values