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 3
Crystal structure of KAT6A^mutCys in complex with AcCoA. (a) shows the overall fold of KAT6A^mutCys (PDB entry 29uq), with the four mutated surface Cys-to-Ser residues shown in stick representation with green C atoms, the co-crystallized cofactor AcCoA with magenta C atoms and the structural zinc ion as an orange sphere. Highlighted in cyan is the P-loop of KAT6A, which wraps around and coordinates the pyrophosphate unit of AcCoA via a series of hydrogen bonds. (b) shows a zoom into the part of the AcCoA-binding pocket where the pyrophosphate unit is coordinated within the P-loop. Residues lining this binding pocket are shown in stick representation. The 2.1 Å resolution 2F_o − F_c electron-density map around the bound cofactor (contoured at 1.3σ) is shown in blue.

STRUCTURAL
BIOLOGY

ISSN: 2059-7983

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

https://doi.org/10.1107/S2059798326008545

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