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Figure 1
Belumosudil complexed with CK2α. (a) The interactions of belumosudil in the ATP site of CK2α observed in the crystal structure. Hydrogen bonds are shown as dashed lines and hydrophobic interactions with wider dashes. (b) The difference electron-density map in the CK2α ATP site, contoured at 2 r.m.s.d., before belumosudil was modelled. The refined structure of the inhibitor is superimposed for reference. (c) The interaction of belumosudil with the hinge region. (d) The hydrophobic residues of the ATP site that sandwich the aromatic ring systems of belumosudil. (e) The bridging water interaction between belumosudil and Lys68. (f) The linker to the flexible tail of belumosudil sticks out of the ATP site into solvent, with part of the tail unmodelled due to a lack of electron density.

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X
Volume 78| Part 10| October 2022| Pages 348-353
https://doi.org/10.1107/S2053230X22008767
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