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. 2021 Mar 2;11:4977. doi: 10.1038/s41598-021-83696-x

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© The Author(s) 2021

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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Structural changes caused by F432S substitution. (A) Evaluation of the Cα RMSD as a function of time for the CD loop (upper plot) and existence map for the hydrogen bond between Arg137 of the C helix and heme propionate (lower plot) are shown. Presence of the R137-heme hydrogen bond is shown by vertical red lines. (B) The positions of the CD loop and D152-R281 salt bridge in superimposed structures of the wild-type CYP1A2 (gray) and F432S (pink). UCSF Chimera 1.11 (www.cgl.ucsf.edu/chimera) was used for superposition and three-dimensional visualization of the structures.