KAT6A–inhibitor co-crystal structures: tackling a challenging crystallization target via two alternative approaches

Puetter, V.; Bouché, L.; Nowak-Reppel, K.; Ferrara, S.J.; Gradl, S.N.; Korr, D.; Strathdee, C.A.; ter Laak, A.; Hillig, R.C.

doi:10.1107/S2059798326008545

Figure 7
Comparative binding-mode analysis over three different inhibitor classes. (a) shows KAT6A^mutCys in complex with the cofactor AcCoA (PDB entry 29uq, C atoms in grey). The P-loop and the beginning of the adjacent helix which coordinate the pyrophosphate unit of the cofactor are shown in magenta. (b) shows the superimposition of KAT6A^mutCys–AcCoA (PDB entry 29ur; C atoms in grey) with KAT6A^mutCys in complex with benzofuran BAY-184 (PDB entry 9fkr; ter Laak et al., 2024

; C atoms in lilac); (c) shows the same superimposition as in (b), but now additionally with the co-complex of KAT6A^mutCys with WM-8014 of the hydrazine-sulfonamide series (PDB entry 29uq; C atoms in yellow). (d) shows the superimposition of KAT6A^mutCys–AcCoA with KAT8^mutant/MYST^cryst in complex with the benzothiadiazine Example 41 (PDB entry 29uu; C atoms in cyan).

STRUCTURAL
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ISSN: 2059-7983

Volume 82| Part 9| September 2026| Pages 1111-1124

https://doi.org/10.1107/S2059798326008545

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