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. 2023 Feb 20;13:2989. doi: 10.1038/s41598-023-30046-8

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© The Author(s) 2023

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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/.

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Docking poses of Best ranked plant secondary metabolites on the acetylcholinesterase crystal structure (PDBid: 1QON). (A) p-cymene; (B) carvacrol; (C) γ-terpinene; (D) Δ³-carene. Acetylcholinesterase' residues are colored according to the atom type of the interacting amino-acid residues (protein’s carbon, pale yellow; oxygen, red; nitrogen, blue). The protein–ligand interactions are represented by dash lines as follows: hydrogen bond interactions are colored in yellow, and -π interactions are colored in blue.