3o8b

X-ray diffraction
1.95Å resolution

Visualizing ATP-dependent RNA Translocation by the NS3 Helicase from HCV

Released:

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:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Core protein precursor Chains: A, B
Molecule details ›
Chains: A, B
Length: 666 amino acids
Theoretical weight: 70.87 KDa
Source organism: Hepatitis C virus subtype 1b
Expression system: Escherichia coli
UniProt:
  • Canonical: Q99AU2 (Residues: 1029-1657; 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: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 91.299Å b: 111.955Å c: 139.927Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.183 0.222
Expression system: Escherichia coli