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. 2019 Dec 12;9:18919. doi: 10.1038/s41598-019-55364-8

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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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Binding and interaction pattern of SCH at the fifth subdomain in the extracellular domain of TrkA receptor. Three-dimensional bound conformation of SCH in the TrkA, where it established direct interactions through hydrogen and hydrophobic bonds (a). Dotted lines represent the type of interactions between binding site residues and ligand. The results of MD simulation inferring as the RMSDs of protein and ligand that describe the overall conformational stability during 50 ns simulation (b). SCH mediated interactions to the binding site residues in TrkA receptor, categorized by hydrogen, hydrophobic and water bridge, respectively (c). Here each bar represents the percent of bond occupancy as a fraction.