1a1q

X-ray diffraction
2.4Å 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

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-150808 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease/helicase NS3 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 189 amino acids
Theoretical weight: 19.89 KDa
Source organism: Hepacivirus hominis
Expression system: Escherichia coli
UniProt:
  • Canonical: P26663 (Residues: 1027-1215; Coverage: 6%)
Sequence domains: Hepatitis C virus NS3 protease

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-3
Spacegroup: R32
Unit cell:
a: 133Å b: 133Å c: 223Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.225 0.225 0.32
Expression system: Escherichia coli