The SARS-CoV-2 helicase (non-structural protein nsp13) has been less studied but has considerable potential for the discovery of drugs against SARS-CoV-2. Of the 16 known CoV nsp proteins, the helicase is essential for viral replication and, not surprisingly, it has the highest sequence conservation across the CoV family. As such, this vital enzyme represents a promising target for anti-CoV drug development as drugs targeting it have the potential to be active against all SARS-CoV-2 strains. The helicase contains 601 amino acids and is part of the superfamily 1B highly conserved within all coronaviruses. Helicases can have either 3'-5' (SF1A subfamily) or 5'-3'(SF1B subfamily) translocation polarity, defined as the direction (characterized as 5'→3' or 3'→5') of helicase movement on the DNA/RNA single-strand along which it is moving . The SARS-CoV-2 helicase is a critical enzyme for viral replication as it initiates the first step of the RNA cap synthesis that is essential to protect the virus from innate immune attack, to stabilize it, and ensure its translation. We previously developed an in silico screening protocol that was used to identify drug repurposing candidates for SARS-CoV-2 M pro and RdRp . The utility of this approach was established by the large numbers of predicted candidates that had experimentally validated activity against SARS-CoV-2 and/or the specific target proteins.