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. 2021 Mar 23;11:6618. doi: 10.1038/s41598-021-85675-8

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© The Author(s) 2021

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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ETD directly binds to Akt. (A) Molecular docking analysis of ETD and Akt was performed by AutoDock4.2 and PyMOL program. (B) A schematic diagram, created by BIOVIA Discovery Studio Visualizer 2017, of the interacting residues between ETD and Akt is shown. Hydrogen bonds are displayed in green. The van der Waals interactions are shown in light green. The anion-π and sulfur-π interactions are shown in orange and yellow, respectively.