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TitleUnmasking the Conformational Stability and Inhibitor Binding to SARS-CoV-2 Main Protease Active Site Mutants and Miniprecursor.
Journal, issue, pagesJ. Mol. Biol., Vol. 434, Page 167876-167876, Year 2022
Publish dateAug 18, 2022 (structure data deposition date)
AuthorsKovalevsky, A. / Coates, L. / Kneller, D.W. / Ghirlando, R. / Aniana, A. / Nashed, N.T. / Louis, J.M.
External linksJ. Mol. Biol. / PubMed:36334779
MethodsX-ray diffraction
Resolution1.8 - 1.9 Å
Structure data

PDB-8e4j:
Room-temperature X-ray structure of SARS-CoV-2 main protease H41A miniprecursor mutant
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-8e4r:
Room-temperature X-ray structure of SARS-CoV-2 main protease H41A miniprecursor mutant in complex with GC373
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-HOH:
WATER

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

Source
  • severe acute respiratory syndrome coronavirus 2
KeywordsHYDROLASE / homodimer / cysteine protease / precursor enzyme / H41A mutation

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