1ns3

X-ray diffraction
2.8Å resolution

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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:
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
hetero tetramer
hetero dimer (preferred)
hetero 24-mer
PDBe Complex ID:
PDB-CPX-150809 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Serine protease/helicase NS3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 186 amino acids
Theoretical weight: 19.8 KDa
Source organism: Hepatitis C virus (isolate BK)
Expression system: Escherichia coli
UniProt:
  • Canonical: P26663 (Residues: 1029-1206; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease
Structure domains:
Non-structural protein 4A Chains: C, D
Molecule details ›
Chains: C, D
Length: 14 amino acids
Theoretical weight: 1.47 KDa
Source organism: Hepatitis C virus (isolate BK)
Expression system: Escherichia coli
UniProt:
  • Canonical: P26663 (Residues: 1678-1689; Coverage: 0%)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P6322
Unit cell:
a: 96.96Å b: 96.96Å c: 167.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.204 0.204 not available
Expression system: Escherichia coli