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. 2020 Feb 5;10:1875. doi: 10.1038/s41598-020-58635-x

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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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Distribution of clinical resistant and susceptible mutations in PncA. (A) Venn diagram representing the distribution of clinical mutations in the different datasets used to build the predictive model. (B) Clinical resistant and susceptible mutations mapped on the crystal structure. Amino acid positions where both susceptible and resistant mutations were seen are colored in cyan and emphasizes the need for a better and improved tool to classify them accurately. (C) Surface view of PncA with the docked PZA (yellow, ball and stick representation). Clinical resistant mutations, shown in red, are not just located at the PZA binding site, but are spread equally throughout the whole protein. (D) Molecular interactions between PZA (yellow sticks) and the surrounding amino acids which are part of the catalytic triad (Asp8) and substrate binding site (Trp68, Phe13). Hydrogen bonds are shown as blue dashes, and π-interactions as green dashes.