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. 2022 Apr 11;12:6065. doi: 10.1038/s41598-022-10028-y

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© The Author(s) 2022

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 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/.

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Comparison of the crystal structures of dmJMJD7 and hsJMJD7. (A) Except for the dimerization interfaces, the overall structures of dmJMJD7 and hsJMJD7 oxygenases adopt similar folds, despite only 45% sequence conservation. The core distorted DSBH fold is highlighted. (B) Views from the active sites of dmJMJD7 and hsJMJD7 showing very similar metal ion (Mn in place of Fe) coordination and co-substrate (2OG) binding modes.