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. 2018 Aug 10;8:11998. doi: 10.1038/s41598-018-30434-5

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© The Author(s) 2018

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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A representation of the in silico substrate competition assays. Overlay of frames for the substrates taken over 25 ns. Cross sections of the dimeric KES23360 (panel a) and N43 (panel b) proteins are shown as a surface, with cofactors in unbound and bound forms (PLP and the HMD:PLP aldimine complex, respectively) shown in a single conformation and in stick representation. AHA molecules are shown as spheres and coloured using a blue/white/red colour scale, relative to their proximity to the centre of the protein. The AHA molecules clearly localise in the active site of the protein in proximity to the cofactors.