RdRp (Nsp12), a conserved protein in coronavirus, is an RNA-dependent RNA polymerase (RdRp) and the vital enzyme of coronavirus replication/transcription complex. The RdRp domain of polymerase is located at the C-terminus and has a conserved Ser-Asp-Asp motif. Nsp8 can de novo synthesize up to 6 nucleotides in length, which can be used as a primer for Nsp12-RdRp RNA synthesis. Further, the Nsp7_Nsp8 complex increases the binding of Nsp12 to RNA and enhances the RdRps enzyme activity of Nsp12. In the research of SARS-CoV and MERS-CoV inhibitors, Nsp12-RdRp has been used as a very important drug target. In principle, targeted inhibition of Nsp12-RdRp could not cause significant toxicity and side effects on host cells, but no specific inhibitors have been found until now.
Based on the protein structure of RdRP, we selected 464 top-ranked docked molecules into RdRP-Targeted compound library (CADD) by molecular docking virtual screening against 15,376 compound structures. To speed up the research and development of anti-SARS-CoV-2 drugs, we provide the virtual screening result for free！
|100 μL * 10 mM (in DMSO)||6600.00|