Inhibitors | Comment | Organism | Structure |
---|---|---|---|
remdesivir | high-affinity and consistent molecular interactions with specific active site residues that anchor remdemsivir within the binding pocket for efficient binding. These residues are Asp452, Thr456, Arg555, Thr556, Val557, Arg624, Thr680, Ser681, and Ser682. Remdesivir binding induces minimal individual amino acid perturbations, subtly interferes with deviations of C-alpha atoms, and restricts the systematic transition of SARS-CoV-2 RNA-dependent RNA polymerase from the buried hydrophobic region to the surface-exposed hydrophilic region. A pharmacophore model based on the observed high-affinity interactions with SARSCoV-2 virus RNA-dependent RNA polymerase is mapped, which showcase the crucial functional moieties of remdesivir and is subsequently employed for virtual screening | Severe acute respiratory syndrome coronavirus 2 |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
nucleoside triphosphate + RNAn | Severe acute respiratory syndrome coronavirus 2 | - |
diphosphate + RNAn+1 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Severe acute respiratory syndrome coronavirus 2 | P0DTD1 | replicase polyprotein 1ab; SARS-CoV-2 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
nucleoside triphosphate + RNAn | - |
Severe acute respiratory syndrome coronavirus 2 | diphosphate + RNAn+1 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RNA-dependent RNA polymerase | - |
Severe acute respiratory syndrome coronavirus 2 |