5e4f

X-ray diffraction
2.1Å resolution

The spring alpha-helix coordinates multiple modes of HCV NS3 helicase action

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'.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease/helicase NS3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 437 amino acids
Theoretical weight: 46.74 KDa
Source organism: Hepatitis C virus (isolate Con1)
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WMX2 (Residues: 1215-1651; Coverage: 15%)
Sequence domains: Flavivirus DEAD domain
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X26C
Spacegroup: P21
Unit cell:
a: 95.451Å b: 46.104Å c: 109.041Å
α: 90° β: 104.05° γ: 90°
R-values:
R R work R free
0.214 0.214 0.252
Expression system: Escherichia coli