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. 2022 Oct 20;13:6234. doi: 10.1038/s41467-022-33858-w

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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 Superposition of the dAHR PAS-B:αNF complex (blue) and mAHR PAS-B:ligand (cyan) docking models. The mAHR PAS-B structure model was created by the program Modeller with the apo dAHR PAS-B structure used as the single template. Ligands are shown in sticks. b Ligand binding property of the dAHR PAS-B M284C/Y336L mutant measured by MST. Data are presented as mean values of two independent experiments. Source data are provided as a Source Data file. c The relative position of the ligand-binding cavity (red surface) of dAHR PAS-B and mAHR PAS-B. Cavity sizes were calculated by the program CASTp using the default probe sphere radius of 1.4 Å. d Cavity comparison of dAHR PAS-B and mAHR PAS-B. Nonconserved residues in the dAHR PAS-B domain are shown in parentheses. A list of mAHR PAS-B residues that evolved from large to small side chains is listed at the bottom.