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. 2023 May 3;617(7960):417–425. doi: 10.1038/s41586-023-06030-7

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© The Author(s) 2023

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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Extended Data Fig. 9 — a. The KOR-GoA displays a different conformation from the 5-HT1BR-miniGo structure, including both TM6 of the receptor and α5 helix of the Gα subunit. b. Comparison of receptor-G protein interface among Gs, Gi1, Gq bound complexes. The TM6 of the receptor, αN and α5 helices of the Gα subunits adopt different conformations. c. The receptor-Gα interface of β2AR-Gαs and 5-HT2AR-Gαq. The dashed lines represent the closest distance between the intracellular receptor residues and the Gα residues. The distance cutoff is 4 Å. The interface area shown in the brackets was calculated by the online server PDBePISA.