Literature summary for 3.4.21.98 extracted from

Love, R.A.; Parge, H.E.; Wickersham, J.A.; Hostomsky, Z.; Habuka, N.; Moomaw, E.W.; Adachi, T.; Hostomska, Z.
The crystal structure of hepatitis C virus NS3 proteinase reveals a trypsin-like fold and a structural zinc binding site (1996), Cell, 87, 331-342.

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Cloned(Commentary)

Cloned (Comment)	Organism
residues 1-189 expressed in Escherichia coli as a soluble protein	Hepacivirus C

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zinc	His149 may be an integral part of zinc coordination, may have a structural rather than a catalytic role, effects on protein folding or post-folding stability	Hepacivirus C

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
20000	-	1 * 20000, NS3 proteinase residues 1-189	Hepacivirus C

Organism

Organism	UniProt	Comment	Textmining
Hepacivirus C	-	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Hepacivirus C

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.05	-	substrate 5A/5B a 15 residue synthetic peptide	Hepacivirus C

Subunits

Subunits	Comment	Organism
monomer	1 * 20000, NS3 proteinase residues 1-189	Hepacivirus C

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Release 2023.1 (January 2023)