X-ray diffraction
2.66Å resolution

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 Chains: A, C
Molecule details ›
Chains: A, C
Length: 200 amino acids
Theoretical weight: 21.23 KDa
Source organism: Hepacivirus C
Expression system: Escherichia coli
  • Canonical: P27958 (Residues: 1027-1207; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
Non-structural protein 4A Chains: B, D
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
  • Canonical: P27958 (Residues: 1677-1696; Coverage: 1%)
Sequence domains: Hepatitis C virus non-structural protein NS4a

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: R32
Unit cell:
a: 223.871Å b: 223.871Å c: 74.962Å
α: 90° β: 90° γ: 120°
R R work R free
0.192 0.192 0.278
Expression systems:
  • Escherichia coli
  • Not provided