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. 2021 Dec 11;19:262. doi: 10.1186/s12915-021-01199-7

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© The Author(s) 2021

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. 1. — Crystal structure of Tet(X4). A Overall structure of Tet(X4) has a conserved FAD-binding motif (dark salmon), a substrate-binding domain (green), and a C-terminal bridge helix (cyan). B The FAD-binding site of Tet(X4), FAD is shown in yellow, and protein carbon atoms are depicted in dark salmon. C Interaction between FAD and Tet(X4). FAD is shown in yellow. Relevant hydrogen bonds are shown as dashed lines and their distances are expressed in Å. The figure was generated by LigPlot+ [14]