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. 2022 Aug 5;5:787. doi: 10.1038/s42003-022-03735-9

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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 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 Structure of ehSMOX with FAD in yellow sticks and MDL72527 in orange sticks. The blue dashed lines represent undefined residues 81–97 (on the left) and 190–210 (in the center). b HDX-MS signature differences between apo hSMOX and hSMOX bound to MDL75257 overlaid onto a putty representation (areas with increased diameter correlate with higher B-factors; the dotted blue line represents residues 190–210) of hSMOX; decreased deuterium uptake upon MDL72527 binding, is depicted with a color spectrum from cyan to dark blue with increased protection.