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. 2019 Nov 11;9:16452. doi: 10.1038/s41598-019-52795-1

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© The Author(s) 2019

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Binding mode of small-molecule ligands to CAMKK2-KD ATP-binding pocket. (A–F) The top part of each panel shows the ligand binding mode to CAMKK2-KD ATP-binding site (shown as molecular surface). Main chain atoms for residues (267–272) within CAMKK2-KD hinge region are represented as sticks. Side-chain atoms for CAMKK2-KD gatekeeper residue (Phe267) and structurally conserved lysine (Lys194) and glutamate (Glu263) residues are also shown as sticks. Black dashed lines represent possible hydrogen bonds between protein, crystallographic water molecules (shown as red spheres) and ligand atoms (shown as stick). The bottom part of each panel shows omit maps for each ligand calculated using SFCHECK³⁶ within the CCP4 suite (contoured at 1.0 σ - gray meshes).