741:{{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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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
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279:– You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.
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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
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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
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This file contains additional information, probably added from the digital camera or scanner used to create or digitize it.
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Permission is granted to copy, distribute and/or modify this document under the terms of the
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164:PubMed: 32155444 DOI: 10.1016/j.cell.2020.02.058
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880:Usage on simple.wikipedia.org
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914:Biến thể Omicron SARS-CoV-2
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964:嚴重急性呼吸道症候群冠狀病毒2型Omicron變異株
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513:copyrighted
283:share alike
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1017:Identifier
996:118.11 dpc
988:118.11 dpc
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704:Dimensions
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622:inception
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730:(689 KB)
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1008:PyMOL
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202:See
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152:PDB
147:WHO
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