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
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-150806 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Polyprotein
Molecule details ›
Chains: A, B
Length: 186 amino acids
Theoretical weight: 19.66 KDa
Source organism: Hepatitis C virus genotype 2
Expression system: Escherichia coli
UniProt:
Structure domains:
Length: 186 amino acids
Theoretical weight: 19.66 KDa
Source organism: Hepatitis C virus genotype 2
Expression system: Escherichia coli
UniProt:
- Canonical:
Q81817 (Residues: 301-480; Coverage: 8%)
Structure domains:
Non-structural protein 4A
Molecule details ›
Chains: C, D
Length: 17 amino acids
Theoretical weight: 1.82 KDa
Source organism: Hepatitis C virus (isolate Japanese)
Expression system: Not provided
UniProt:
Length: 17 amino acids
Theoretical weight: 1.82 KDa
Source organism: Hepatitis C virus (isolate Japanese)
Expression system: Not provided
UniProt:
- Canonical: P26662 (Residues: 1678-1691; Coverage: 1%)
