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. 2019 Mar 1;9:3231. doi: 10.1038/s41598-019-39771-5

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© The Author(s) 2019

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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Ginsenoside binding pocket consists of interactions with D318, N100 and S60 residues in hP2X7 lower body region. (A) An individual subunit is displayed with two lower body region β-sheets highlighted in magenta (β2 and β14). CK is shown docked into the putative binding site. Rotation of this individual subunit by 90° allows better visualisation of the internal loop containing N100 that is predicted to make contact with the glucopyranose ring of ginsenoside CK. (B) Trimeric view of the hP2X7 model showing the docked ginsenoside connecting inter-subunit β-sheets β2 (magenta) and β14 (salmon pink). (C) Closer view of the docked ginsenoside CK displaying interacting residues predicted to make polar contacts; D318, N100 and S60.