Fig. 1: Chemical structure of BMS794833 and the X-ray crystal structure bound to MERTK.
From: BMS794833 inhibits macrophage efferocytosis by directly binding to MERTK and inhibiting its activity
a The chemical structure of BMS794833. b BMS794833 occupies the kinase domain binding pockets from the ATP-binding pocket to the allosteric back pocket. The 2mFo-DFc omit map is shown with a 1.5 σ contour level; BMS794833 showed good occupancy within the MERTK kinase domain. c The interacting hydrogen bonds between the MERTK kinase domain and BMS794833 are depicted as blue dashed lines, and hydrophobic interactions are depicted as yellow dashed lines. d The surface representation of the entrance region of the allosteric back pocket, also known as the hydrophobic patch. Left, the representation of hydrophobicity generated by a “color_h” script based on the previously defined hydrophobicity scale (left)48. Right, the representation of qualitative electrostatic potential by the “vacuum electrostatics” command in the program PyMOL.
