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. 2020 Mar 2;20:67. doi: 10.1186/s12906-020-2859-z

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© The Author(s). 2020

Open AccessThis 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/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 6 — Docking study of the compounds with ketosynthase domain of polyketide synthase protein in A. fumigatus. a Structure of hexadecanoic acid, cis-9-hexadecenal, isoeugenol and elemicin, (b) structure of ketosynthase domain of polyketide synthase protein was retrived from Swiss-model, (c) protein- ligand interactions analysed by LigPlot. Dashed lines indicate hydrogen bonds between the atoms involved. The arc with spokes towards the ligand atoms shows the hydrophobic interaction. Hexadecanoic acid, cis-9-hexadecenal and isoeugenol form proper hydrogen bonding whereas elemicin shows hydrophobic interaction only