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. Author manuscript; available in PMC: 2018 Oct 15.
Published in final edited form as: Cancer Res. 2018 Jan 30;78(8):2096–2114. doi: 10.1158/0008-5472.CAN-17-2870

Figure 3. Structure of MRCKβ in complex with BDP8900 and BDP9066.

Figure 3

(A) BDP8900 or (B) BDP9066 bound to the MRCKβ ATP-binding site in stereo views. Protein residues (grey) are labelled with the single-letter amino acid code and residue number, selected water molecules are indicated by red spheres. Ligands are shown in purple with σA-weighted |Fo|-|Fc|,ϕc electron density maps calculated prior to the initial inclusion of the ligand in refinement contoured at 3.0σ (dark blue). Potential hydrogen bonds are highlighted by dotted black lines. (C) Detailed view of the BDP9066 spiro moiety. The ligand is shown in cyan with a semitransparent surface. (D) Comparison of the binding modes of BDP9066 (cyan) and BDP5290 (blue, PDB ID 4UAL). Protein residues, pocket waters and potential hydrogen bonds are shown as before and colored to match the ligand.