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Literature summary for 3.4.21.98 extracted from

  • Rimmert, B.; Sabet, S.; Ackad, E.; Yousef, M.S.
    A 3D structural model and dynamics of hepatitis C virus NS3/4A protease (genotype 4a, strain ED43) suggest conformational instability of the catalytic triad: implications in catalysis and drug resistivity (2014), J. Biomol. Struct. Dyn., 32, 950-958.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
3D structural model threaded through a template crystal structure of HCV-1b NS3 protease. The model protease has rigid structural features. Local dynamics and 4D analysis of the interactions between the catalytic triad residues His57, Asp81, and Ser139 indicate conformational instability of the catalytic site in HCV-4a NS3 protease Hepacivirus C

Organism

Organism UniProt Comment Textmining
Hepacivirus C
-
genotype 4a
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Hepacivirus C ED43
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genotype 4a
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Synonyms

Synonyms Comment Organism
NS3/4A protease
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Hepacivirus C