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. 2022 May 19;13:2770. doi: 10.1038/s41467-022-30430-4

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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 Conformational changes of the nucleotide-binding site between the closed (gray) and the pre-open (green) states of H175K_cryo-EM. The ADP bound in the closed state is shown as sticks in orange. b Close-up view of the nucleotide-binding site boxed in (a). c Bottom view of the Kir6.2 CTD. The rotation angle between CTDs was measured using Cα positions of L356 of Kir6.2 as marker atoms (shown as spheres).