Function and Biology Details
Reactions catalysed:
Hydrolysis of four peptide bonds in the viral precursor polyprotein, commonly with Asp or Glu in the P6 position, Cys or Thr in P1 and Ser or Ala in P1'.
NTP + H(2)O = NDP + phosphate
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109765 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Polyprotein
Molecule details ›
Chains: A, B
Length: 200 amino acids
Theoretical weight: 21.23 KDa
Source organism: Hepacivirus hominis
Expression system: Escherichia coli
UniProt:
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
Length: 200 amino acids
Theoretical weight: 21.23 KDa
Source organism: Hepacivirus hominis
Expression system: Escherichia coli
UniProt:
- Canonical:
B2Y2M9 (Residues: 1027-1207; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
19-mer peptide from Genome polyprotein
Molecule details ›
Chains: C, D
Length: 23 amino acids
Theoretical weight: 2.39 KDa
Source organism: Hepacivirus hominis
Expression system: Not provided
UniProt:
Length: 23 amino acids
Theoretical weight: 2.39 KDa
Source organism: Hepacivirus hominis
Expression system: Not provided
UniProt:
- Canonical: Q6GYR8 (Residues: 1682-1700; Coverage: 1%)
