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Structure paper

TitleThe P132H mutation in the main protease of Omicron SARS-CoV-2 decreases thermal stability without compromising catalysis or small-molecule drug inhibition.
Journal, issue, pagesCell Res., Vol. 32, Page 498-500, Year 2022
Publish dateJan 24, 2022 (structure data deposition date)
AuthorsSacco, M.D. / Hu, Y. / Gongora, M.V. / Meilleur, F. / Kemp, M.T. / Zhang, X. / Wang, J. / Chen, Y.
External linksCell Res. / PubMed:35292745
MethodsX-ray diffraction
Resolution2.05 Å
Structure data

PDB-7tob:
Crystal structure of the SARS-CoV-2 Omicron main protease (Mpro) in complex with inhibitor GC376
Method: X-RAY DIFFRACTION / Resolution: 2.05 Å

Chemicals

ChemComp-K36:
(1S,2S)-2-({N-[(benzyloxy)carbonyl]-L-leucyl}amino)-1-hydroxy-3-[(3S)-2-oxopyrrolidin-3-yl]propane-1-sulfonic acid / medication, antivirus*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-HOH:
WATER

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN/INHIBITOR / omicron / main protease / 3cl / 3-chemotrypsin like protease / sars-cov-2 / COVID / GC376 / inhibitor / covalent / antiviral / NSP5 / VIRAL PROTEIN / VIRAL PROTEIN-INHIBITOR complex

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