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. 2020 Nov 30;39:265. doi: 10.1186/s13046-020-01775-9

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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 — Computational analysis and predictive modelling of discovery of small molecule inhibitors of KLF7-DNA interaction interface. a The predicted model structure of the zinc-finger domain of KLF7. The overall fold of KLF7 monomer in complex with DNA is presented as a cartoon model. Zinc ions are shown as orange spheres. b Representation of the most preferable druggable site in KLF7. The binding pocket, identified by SiteMap and metaPocket, is shown as solvent surface, coloured by atom charge. c Overlay of the top three compounds. Compound#1 (yellow), Compound#2 (violet), Compound#3 (orange). Main interacting residues for the three scaffolds are displayed