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. 2022 Oct 22;12:17796. doi: 10.1038/s41598-022-22668-1

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© The Author(s) 2022

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Comparative stability and solvent accessibility surface area of the binding site of KRAS^G12D upon the binding of MRTX1133 and the holo protein. (A) Shows the RMSD plots of the C-a atoms of the binding site residues indicating MRTX1133 binding stabilized the residues (red) relative to the holo (black). (B) Shows the SASA plots of the binding site residues indicating a reduction in surface area availability upon MRTX1133 binding (red) relative to the holo protein (black). (C) Shows the hydrophobicity of the binding site. (D) Shows the solvent accessible of area of the binding site.