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. 2019 May 21;10:2261. doi: 10.1038/s41467-019-08620-4

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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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Fig. 5 — Structure of G150 bound to apo h-cGAS^CD. a Chemical formula of G150. b Crystal structure of G150 bound to apo h-cGAS^CD. The bound G150 is shown in a space-filling representation, and the binding pocket is boxed. c 2Fo–Fc electron density map of bound G150 contoured at 1.2 σ level. The electron density is partly defined for the hydroxyl-ethanone side chain attached to the non-planar six-membered ring. d Two views of G150 positioned in its binding pocket within h-cGAS^CD with the protein shown in an electrostatic surface representation. Electrostatic surface potentials were calculated with Coulombic Surface tool in Chimera with thresholds ±10 kcal mol⁻¹ e⁻¹. e Intermolecular contacts and key distances between G150 and amino acids lining the binding pocket of h-cGAS^CD. Distances are in angstrom. Red dashed lines indicate hydrogen bond. f Superposition of the structures of G108 (light blue) and G150 (yellow) as observed in their complexes with h-cGAS^CD. Note that G150 is positioned deeper in the binding pocket than G108 so that the pair of chlorine atoms do not superposition with each other