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![[Figure 2]](wa5155fig2mag.jpg)
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Figure 2
Crystal structure of the PAK4 kinase domain in complex with KPT-7523. (a) Overall structure of PAK4 showing KPT-7523 bound at two distinct sites: (1) the adenine-binding site of ATP (ligand shown in yellow–orange) within the N-lobe (lime) and (2) a substrate-binding site (ligand shown in yellow) within the C-lobe (forest). The N- and C-terminal regions are labeled for orientation. For reference, an ATP molecule from a previously reported structure (PDB entry 4xbr) is overlaid in silver. (b) Close-up view of the adenine-binding site of ATP showing KPT-7523 (yellow–orange) stabilized by hydrogen bonds (purple dashed lines) and hydrophobic interactions. (c) Close-up view of the substrate-binding site with KPT-7523 (yellow) engaged in key hydrogen-bonding and hydrophobic contacts with surrounding residues. (d) Structural superposition of the Boltz-2-generated complex model (green) onto the experimental crystal structure (yellow–orange). The computational model accurately reproduces the experimentally observed KPT-7523 pose at the entry of the ATP-binding cleft (see the supporting information for details). |
![[Figure 2]](wa5155fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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