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Positions of mutations in the SARS-CoV-2 Omicron variant compared to the original strain, showing amino acid substitutions (yellow), deletions (red), and insertions (green). In this trimeric structure, two monomers (gray and light blue) have their receptor-binding domains in the "down" conformation while one (dark blue) is in the "up" or "open" conformation. "Top" view is looking toward the membrane and shows the receptor-binding domains. Mutation data source from WHO. Rendered from PDB: 6VYB​.

Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Walls, A.C., Park, Y.J., Tortorici, M.A., Wall, A., McGuire, A.T., Veesler, D. (2020) Cell 181: 281

PubMed: 32155444 DOI: 10.1016/j.cell.2020.02.058
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Author Opabinia regalis
Other versions See File:Spike omicron mutations side.png for side view

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current04:25, 29 November 2021Thumbnail for version as of 04:25, 29 November 20211,280 × 960 (689 KB)Opabinia regalis{{Information |Description=Positions of mutations in the SARS-CoV-2 Omicron variant compared to the original strain, showing amino acid substitutions (yellow), deletions (red), and insertions (green). In this trimeric structure, two monomers (gray and light blue) have their receptor-binding domains in the "down" conformation while one (dark blue) is in the "up" or "open" conformation. Mutation data source from [https://www.who.int/news/item/26-11-2021-classification-of-omicron-(b.1.1.529)-sar...

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