1cu1

X-ray diffraction
2.5Å resolution

CRYSTAL STRUCTURE OF AN ENZYME COMPLEX FROM HEPATITIS C VIRUS

Released:

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:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-150815 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease/helicase NS3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 645 amino acids
Theoretical weight: 68.57 KDa
Source organism: Hepacivirus hominis
Expression system: Escherichia coli
UniProt:
  • Canonical: P26663 (Residues: 1678-1657; Coverage: 21%)
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS
Spacegroup: P212121
Unit cell:
a: 91.36Å b: 110.51Å c: 141.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.2 0.26
Expression system: Escherichia coli