The exact molecular mechanism of remdesivir's action against SARS‐CoV‐2 has recently been elucidated by Yin et al. 219  who reported cryo‐EM structures of SARS‐CoV‐2 RdRP with remdesivir monophosphate (RMP) covalently bound to the primer strand. As only a single RMP was incorporated in each observed primer strand the inhibition mechanism was shown to be nonobligate RNA chain termination. The addition of RTP led to a complete inhibition of RNA polymerization activity at a concentration of 1 mM, even in the presence of ATP in high concentrations of 100 mM. The authors further highlight the high conservation level of catalytic sites of RdRPs in different RNA viruses, which makes the discovery of future broad‐spectrum antiviral RdRP inhibitors seem likely.