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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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Cluster analysis performed on AHA molecules with from the N16 system. The centroids are coloured according to the active site they ultimately occupy, with those occupying the ‘empty’ site in yellow and the ‘occupied’ site in pink (panel a). The monomers comprising the protein dimer are coloured cyan and green and the boxed area highlights the region of the surface over which both trajectories converge. (Panel b) Closer analysis and comparison of the boxed region showing non-conserved residues that contribute to an open or closed channel through which substrate appears to move. In KES23360, E178 appears to dam the channel, whilst in N16/N43 the corresponding D178 does not. Other non-conserved residues in the region (positions 142 and 179) are highlighted in white with heteroatoms coloured (O – red, N – blue), and labelled accordingly. A sequence alignment of the region is also shown.