BIOL 244 - Mpro SARS-CoV-19 with Inhibitor N3.

Mpro, the main, chymotrypsin-like protease of the SARS-CoV-2 virus is an ideal target for drug treatments due to its major role in processing polyproteins, for viral replication and RNA transcription. The structure of the Mpro features an antiparallel β-barrel motif, made up of Domains I (residues S1–P102) and II (residues A103-P184), And Domain III (residues T201–Q306), made up of a motif of five α-helices (α5–α9) which form a compact globular structure. Domain III is joined by a long loop (residues F185–I200) to Domain II. The substrate-binding pocket of the Mpro is located in the chymotrypsin-like fold between Domain I and Domain II. The pocket contains the catalytic dyad, H41 and C145. This is the main binding location of the inhibitor N3, a broad spectrum inhibitor.