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. 2015 Jun 29;6(8):913–918. doi: 10.1021/acsmedchemlett.5b00174

Figure 2.

Figure 2

X-ray structure of 13 bound to MAP4K4 at 2.89 Å (PDB: 4ZK5). Select hydrogen bond (red), pi stacking (orange), and van der Waals (yellow) interactions are highlighted. Proximal ordered waters are shown in cyan spheres. The solvent-accessible protein surface in the vicinity of the ligand is shown in white, demonstrating the extensive contribution to the constricted enclosure created by the approach of Tyr36 enabled by a buckled P loop conformation. The ligand emerges toward solvent at the left, where the azetidine moiety creates a bend around the Phe107 side chain to maintain close contacts to the protein surface.