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. 2017 Nov 27;7:16338. doi: 10.1038/s41598-017-15997-z

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© The Author(s) 2017

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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Cysteine modification in human kinases. (a) Predicted cysteine pKas for a non-redundant set of human protein kinases, with red and blue arrows marking pKa decreased or increased, respectively, from the model compound pKa of cysteine (8.3). (b) Kinase domains of 4 kinases (3v5l A, 4rx5 A, 3pozA, 3pjcA) are aligned, with colour coding of cysteines according to a predicted lowering (red, more reactive) or raising (blue) of the sidechain pKa. Accessibility of each cysteine is marked as ‘a’ (accessible) or ‘b’ (buried). (c) EGFR kinase domain is shown for 3poz chain A, with inhibitor (green), and reactive cysteine site (red) at an α-helix amino-terminus.