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Literature summary for 3.4.21.98 extracted from

  • Abian, O.; Vega, S.; Neira, J.L.; Velazquez-Campoy, A.
    Conformational stability of hepatitis C virus NS3 protease (2010), Biophys. J., 99, 3811-3820.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
Zn2+ zinc-dependent serine protease. zinc ion is not involved in the catalytic mechanism but it is essential for the structural integrity of the protein. The global unfolding heat capacity is dominated by the zinc dissociation step, suggesting that the binding of zinc induces a significant structural rearrangement of the protein. Contrary to other homologous zinc-dependent proteases, the zinc-free NS3 protease is not completely unstructured Hepacivirus C

Organism

Organism UniProt Comment Textmining
Hepacivirus C
-
-
-

Synonyms

Synonyms Comment Organism
NS3 protease
-
Hepacivirus C