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. 2019 Feb 7;9:1600. doi: 10.1038/s41598-018-35835-0

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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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Illustration of Hsp90α in the open conformation. (A) The location of the different binding site residues are shaded: Site-1 helix_18-19 (red), helix_21-22 four-helix bundle (yellow) and Site-2 sub-pocket (blue). The NTD location of ATP and magnesium ions (spheres) are also shown. (B) Hsp90’s nucleotide driven conformational cycle (Adopted from Penkler et al.³⁷). (C) Inset – zoomed in view of docked compounds SANC309 red, SANC491 green, SANC518 blue, and Novobiocin magenta.