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. 2019 Dec 17;10:5759. doi: 10.1038/s41467-019-13652-x

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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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Fig. 3 — a Surface representation of PRDM9 PR domain (white) bound by SAM (blue) and MRK-740. b Intermolecular interactions between MRK-740 and its binding pocket. Hydrophobic interactions (light blue), pi–pi interactions (yellow), CH–pi interactions (pink) and polar interactions (green) are represented by dashes. Structural alignment with the mouse holoenzyme (PDB accession code 4C1Q) showing steric clashes between MRK-740 and (c) the substrate lysine residue (green) and (d) the post-SET substrate recognition helix when in an active, substrate-bound conformation (orange). The corresponding helix in the inhibited, human structure is shown in (teal).