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. 2018 Mar 21;9:1180. doi: 10.1038/s41467-018-03410-w

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© The Author(s) 2018

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 — Stereoviews of JMJD5.substrate complexes showing likely productive and non-productive arginine-binding modes. a JMJD5.Mn.NOG.RPS6 (Complex 1, PDB: 6F4P), b JMJD5(Q275C).Mn.NOG.RPS6(A138C) (Complex 2, PDB: 6F4Q), c JMJD5(N308C).Mn.NOG.RCCD1 (Complex 3, PDB: 6F4R), d JMJD5(N308C).Mn.2OG.RCCD1 (Complex 4, PDB: 6F4S) and e JMJD5(W414C).Mn.NOG.RCCD1 (Complex 5, PDB: 6F4T). The target arginine in both RPS6 (R137) and RCCD1 (R141) binds in a shallow channel on the JMJD5 surface forming hydrophobic interactions with Y243/W310 and hydrogen bonds with E238/ S318 in both 'productive' (Complex 1/A, Complex 3 and Complex 4) and 'non-productive' (Complex 1/B, Complex 2 and Complex 5) conformations. 2F_o−F_c (grey meshes) for JMJD5 and difference electron density (F_o−F_comit map, blue) for substrates are contoured to 1.2−1.5σ and 3σ, respectively. Red arrows indicate hydroxylated C–H bonds