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TitleStructural basis of human ACE2 higher binding affinity to currently circulating Omicron SARS-CoV-2 sub-variants BA.2 and BA.1.1.
Journal, issue, pagesCell, Vol. 185, Page 2952-2960.e10, Year 2022
Publish dateMar 19, 2022 (structure data deposition date)
AuthorsLi, L. / Liao, H. / Meng, Y. / Li, W. / Han, P. / Liu, K. / Wang, Q. / Li, D. / Zhang, Y. / Wang, L. ...Li, L. / Liao, H. / Meng, Y. / Li, W. / Han, P. / Liu, K. / Wang, Q. / Li, D. / Zhang, Y. / Wang, L. / Fan, Z. / Zhao, X. / Sun, Y. / Huang, N. / Qi, J. / Gao, G.F.
External linksCell / PubMed:35809570
MethodsX-ray diffraction
Resolution2.7 - 3 Å
Structure data

PDB-7xaz:
Crystal structure of Omicron BA.1.1 RBD complexed with hACE2
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-7xb0:
Crystal structure of Omicron BA.2 RBD complexed with hACE2
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-7xb1:
Crystal structure of Omicron BA.3 RBD complexed with hACE2
Method: X-RAY DIFFRACTION / Resolution: 2.7 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
KeywordsHYDROLASE/VIRAL PROTEIN / SARS-CoV-2 / Omicron / RBD / ACE2 / complex structure / VIRUS / VIRAL PROTEIN / HYDROLASE-VIRAL PROTEIN complex / hACE2

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