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. 2020 Jul 20;10:11992. doi: 10.1038/s41598-020-68950-y

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© The Author(s) 2020

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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KRAS(G12C)–AMG 510 structure. (A) Chemical structure of AMG 510. (B) Crystal structure of KRAS(G12C)–AMG 510 complex (PDB ID: 6oim). AMG 510 (green) binds to the SII-P and exploits a cryptic pocket formed by H95/Y96/Q99. (C) B-factor values of KRAS(G12C)–AMG 510 structure. Thick and red ribbon indicate a high B-factor value, whereas thin and blue a low value. Cα-atoms of start and end residues of higher B-factor regions are highlighted with cyan spheres (regions: G0–T2; F28–T35; Y40–S51; A59–R68; H95–P110; L120–V125; I163–H166). A disordered region of the structure, D105–E107, is indicated with dashed red line. (D) Observed crystal contacts in KRAS(G12C)–AMG 510 structure. Residues within 4 Å of the protein are shown in sticks together with their molecular surface (yellow). In (B, D) KRAS switch regions: switch-I: residues 25–40 and switch-II: residues 58–72 are highlighted with red and blue, respectively. C12 is highlighted with orange.