Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
nucleoside triphosphate + RNAn | Severe acute respiratory syndrome coronavirus 2 | the enzyme plays a crucial role in SARS-CoV-2 replication | 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 | the enzyme plays a crucial role in SARS-CoV-2 replication | Severe acute respiratory syndrome coronavirus 2 | diphosphate + RNAn+1 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RDRP | - |
Severe acute respiratory syndrome coronavirus 2 |
RNA-dependent RNA polymerase | - |
Severe acute respiratory syndrome coronavirus 2 |
General Information | Comment | Organism |
---|---|---|
drug target | the enzyme plays a crucial role in SARS-CoV-2 replication, and thus could be a potential drug target. Comprehensive computational approaches including drug repurposing and molecular docking are employed to predict an effective drug candidate targeting RdRp of SARS-CoV-2. This study reveales that Rifabutin, Rifapentine, Fidaxomicin, 7-methyl-guanosine-5'-triphosphate-5'-guanosine and Ivermectin have a potential inhibitory interaction with RNA-dependent RNA polymerase (RdRp) of SARS-CoV-2 and could be effective drugs for COVID-19. Virtual screening of the compounds from ZINC database allow the prediction of two compounds (ZINC09128258 and ZINC09883305) with pharmacophore features that interact effectively with RdRp of SARSCoV-2, indicating their potentiality as effective inhibitors of the enzyme. Comparative structural analysis of protein-inhibitor complexes reveals that the amino acids Y32, K47, Y122, Y129, H133, N138, D140, T141, S709 and N781 are crucial for drug surface hotspot in the RdRp of SARS-CoV-2 | Severe acute respiratory syndrome coronavirus 2 |
physiological function | the enzyme plays a crucial role in SARS-CoV-2 replication | Severe acute respiratory syndrome coronavirus 2 |