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 Mpro 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 Mpro, 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.
Highlights
The COVID-19 disease caused by the syndrome coronavirus (SARS)-CoV-2 coronavirus has become a pandemic health crisis
We present here atomic details pertinent to the function and inhibitor binding to SARS-CoV-2 3CL Mpro
We grew large crystals (Supplementary Fig. 1) that could be used on a home source to ensure minimal radiation damage
Summary
The COVID-19 disease caused by the SARS-CoV-2 coronavirus has become a pandemic health crisis. The catalytic residues Cys[145] and His[41] in 3CL Mpro are buried in an active site cavity located on the surface of the protein. Results Atomic details of 3CL Mpro active site at room temperature.
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