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. 2022 May 31;32(7):609–620. doi: 10.1038/s41422-022-00672-4

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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. 6 — a Overall structure of the BA.2-RBD and mACE2 complex. b Details of the binding between BA.2-RBD and mACE2. The binding between BA.2-RBM and mACE2 consists mainly of two interaction regions, marked in a red or a blue box. Residues involved in the interactions are shown as sticks. Hydrogen bonds are shown as dashed black lines. c, d Overall structure of the BA.1-RBD and mACE2 complex, with detailed hydrogen bond or salt bridge interactions in BA.1-RBD and ACE2 interface with the same view as in (a, b). e, f The superposition of the BA.2 RBD and mACE2 complex with SARS-CoV-2 WT-RBD alone (PDB: 6LZG). Detailed hydrogen bond or salt bridge interactions are highlighted with the same view as in a, b.