Figure 4. Key allo-residues predicted in BCR-ABL1.

(A) The crystal structure of the kinase domain of BCR-ABL1. The allosteric inhibitor asciminib, represented by sticks, binds to the myristoyl pocket (marine). (B) Predicted key allo-residues in the myristoyl pocket. The predicted key allo-residues are represented by marine sticks. One of the predicted key allo-residues, L359, forms a favorable hydrophobic interaction with a fluorine atom in asciminib, represented by a red dashed line. Water is represented by a red sphere. (C) The structure of fragment-derived hit 4 and hit 5 and the final marketed drug asciminib.