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. 2022 Sep 16;13:5444. doi: 10.1038/s41467-022-33174-3

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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. 2 — a Side view of the overall structure of Rac1 (cartoon, gold) binding to the D site (semitransparent surface, green). F37 and Y967 side chains are shown as reference points. b Top view and semitransparent surface charge representation of the D site (calculated using APBS in Pymol⁴⁵), showing key interactions between Sra1 and Rac1. Yellow dotted lines indicate polar interactions. White dashed line indicates binding surface boundary. For clarity, the backbones of Switch I and II are shown as loops. c, d Structural comparison of Rac1 and the D site in the bound (dark colors) and unbound (light colors, PDB 3SBD for Rac1) states. Curved arrows indicate side chain flipping upon Rac1 binding. Straight arrow indicates translation of polypeptide backbone. Black dashed lines indicate the interdigitated π-π stacking.