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. 2020 Feb 28;10:3731. doi: 10.1038/s41598-020-60617-y

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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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Homology model of Asc-1 in the outward-open occluded conformation before and after docking d-serine. TM1 et TM6 are colored as in Fig. 3. (a) Side view of the OOO conformation. (b) Zoom on the top view of the OOO conformation after docking d-serine. Similar bindings are observed as in Fig. 3 between the backbone of TM1, TM6, TM8 and the amino acid moiety of the substrate. Specific vdw and H-bound contacts are also observed between TM6, TM8 and d-serine side chain. (c) A 2D diagram of interactions between the Asc-1 OOO model and d-serine.