Inhibitors | Comment | Organism | Structure |
---|---|---|---|
remdesivir triphosphate | the inhibition mechanism of remdesivir triphosphate is inestigated through structural and kinetic analyses | 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 | - |
? | |
nucleoside triphosphate + RNAn | cryo-EM structures of the SARS-CoV-2 RNA polymerase in complexes with RNA, before and after RNA translocation, reveals structural rearrangements that the RNA-dependent RNA polymerase (RdRp) nsp12 and its co-factors (nsp7 and nsp8) undergo to accommodate nucleic acid binding | Severe acute respiratory syndrome coronavirus 2 | diphosphate + RNAn+1 | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | a transition model from the nsp7-nsp8 hexadecameric primase complex to the nsp12-nsp7-nsp8 polymerase complex is proposed to provide clues for the understanding of the coronavirus transcription and replication machinery | Severe acute respiratory syndrome coronavirus 2 |
Synonyms | Comment | Organism |
---|---|---|
nsp12 | - |
Severe acute respiratory syndrome coronavirus 2 |
RDRP | - |
Severe acute respiratory syndrome coronavirus 2 |
RNA-dependent RNA polymerase | - |
Severe acute respiratory syndrome coronavirus 2 |
SARSCoV-2 polymerase | - |
Severe acute respiratory syndrome coronavirus 2 |