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. 2023 Jul 10;14:4090. doi: 10.1038/s41467-023-39742-5

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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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Fig. 4 — a Cross section of the F₁ domain in 81° showing the catalytic sites viewed from the F_o side. The bound nucleotides are represented as spheres. The electron density of the nucleotides within the enclosed circles are shown in larger view on the right. The distance between γ (or Pi) and β phosphate of the ATP in each conformational state is shown in blue (Å). Each distance was calculated using Chimera software. b Cross section of the F₁ domain in ATP-waiting (120°). c Comparison of the Pi binding site in α_Eβ_E in the 91° and 120° structures with electron density indicated for the Pi. d Comparison of the catalytic site of the α_Eβ_E in ATP waiting (cream) and step waiting (purple). ATP in step waiting is represented by the orange and blue sticks. The step waiting structure was captured at high [ATP].