Function and Biology Details
Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
NTP + H(2)O = NDP + phosphate
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'.
ATP + H(2)O = ADP + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero tetramer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease/helicase NS3
Molecule details ›
Chains: A, C
Length: 200 amino acids
Theoretical weight: 21.23 KDa
Source organism: Hepacivirus C
Expression system: Escherichia coli
UniProt:
Structure domains:
Length: 200 amino acids
Theoretical weight: 21.23 KDa
Source organism: Hepacivirus C
Expression system: Escherichia coli
UniProt:
- Canonical:
P27958 (Residues: 1027-1207; Coverage: 6%)
Structure domains:
Non-structural protein 4A
Molecule details ›
Chains: B, D
Length: 23 amino acids
Theoretical weight: 2.39 KDa
Source organism: Hepatitis C virus (isolate H77)
Expression system: Not provided
UniProt:
Length: 23 amino acids
Theoretical weight: 2.39 KDa
Source organism: Hepatitis C virus (isolate H77)
Expression system: Not provided
UniProt:
- Canonical: P27958 (Residues: 1677-1696; Coverage: 1%)
