First, we designed an novel ensemble docking approach derived from crystal structures and implemented with extensive sampling using volunteer distributed computation, 1) to compare the binding location, affinity and stability of the active forms tenofovir-diphosphate (which is comparable to a triphosphate, as tenofovir prodrug already contains one phosphate residue), remdesivir-triphosphate, and deoxyadenosine triphosphate (dATP) with the RdRp-CoV-2- RNA chain complex, 2) to determine the capability of active tenofovir to bind to the RdRp-CoV-2 in order to terminate RNA polymerization, to 3) compare the binding energy and site with that of remdesivir, and 4) to determine potential limitations arising from their molecular structures.