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Literature summary extracted from

  • Mittal, L.; Kumari, A.; Suri, C.; Bhattacharya, S.; Asthana, S.
    Insights into structural dynamics of allosteric binding sites in HCV RNA-dependent RNA polymerase (2020), J. Biomol. Struct. Dyn., 38, 1612-1625 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.48 anthranilic acid
-
 Hepacivirus C
2.7.7.48 benzimidazole
-
 Hepacivirus C
2.7.7.48 cyclopropylindolobenzazepine inhibitors
-
 Hepacivirus C
2.7.7.48 dihydropyranone inhibitor binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules Hepacivirus C
2.7.7.48 indole
-
 Hepacivirus C
2.7.7.48 indole diamide inhibitors
-
 Hepacivirus C
2.7.7.48 indole-N-acetamide inhibitors
-
 Hepacivirus C
2.7.7.48 indolo-benzoxazocine inhibitors
-
 Hepacivirus C
2.7.7.48 Isoquinoline
-
 Hepacivirus C
2.7.7.48 phenylalanine binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules Hepacivirus C
2.7.7.48 tetracyclic indole inhibitors
-
 Hepacivirus C
2.7.7.48 thiazolone inhibitors
-
 Hepacivirus C
2.7.7.48 thiophene binding of non-nucleoside inhibitors induces significant fluctuations at the atomic level which are critical for enzymatic activity, with minimalglobal structural alterations. Residue-wise mapping of interactions of non-nucleoside inhibitors at different sites exhibits some conserved interaction patterns of key amino acids and water molecules Hepacivirus C

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.48 nucleoside triphosphate + RNAn Hepacivirus C
-
 diphosphate + RNAn+1
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.48 Hepacivirus C O92972 genome polyprotein
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.48 nucleoside triphosphate + RNAn
-
 Hepacivirus C diphosphate + RNAn+1
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.7.48 RDRP
-
 Hepacivirus C
2.7.7.48 RNA-dependent RNA polymerase
-
 Hepacivirus C

General Information

EC Number General Information Comment Organism
2.7.7.48 drug target inhibition of the viral RNA-dependent RNA polymerase (RdRp) to resolve chronic infection is a useful therapeutic strategy against Hepatitis C virus Hepacivirus C