6WQF
Structural Plasticity of the SARS-CoV-2 3CL Mpro Active Site Cavity Revealed by Room Temperature X-ray Crystallography
Summary for 6WQF
| Entry DOI | 10.2210/pdb6wqf/pdb |
| Descriptor | 3C-like proteinase (2 entities in total) |
| Functional Keywords | sars-cov-2 main protease, viral protein, hydrolase |
| Biological source | Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) |
| Total number of polymer chains | 1 |
| Total formula weight | 33825.55 |
| Authors | Kneller, D.W.,Kovalevsky, A.,Coates, L. (deposition date: 2020-04-28, release date: 2020-05-06, Last modification date: 2023-10-18) |
| Primary citation | Kneller, D.W.,Phillips, G.,O'Neill, H.M.,Jedrzejczak, R.,Stols, L.,Langan, P.,Joachimiak, A.,Coates, L.,Kovalevsky, A. Structural plasticity of SARS-CoV-2 3CL Mproactive site cavity revealed by room temperature X-ray crystallography. Nat Commun, 11:3202-3202, 2020 Cited by PubMed Abstract: The COVID-19 disease caused by the SARS-CoV-2 coronavirus has become a pandemic health crisis. An attractive target for antiviral inhibitors is the main protease 3CL M due to its essential role in processing the polyproteins translated from viral RNA. Here we report the room temperature X-ray structure of unliganded SARS-CoV-2 3CL M, revealing the ligand-free structure of the active site and the conformation of the catalytic site cavity at near-physiological temperature. Comparison with previously reported low-temperature ligand-free and inhibitor-bound structures suggest that the room temperature structure may provide more relevant information at physiological temperatures for aiding in molecular docking studies. PubMed: 32581217DOI: 10.1038/s41467-020-16954-7 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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