1hei

X-ray diffraction
2.1Å resolution

STRUCTURE OF THE HEPATITIS C VIRUS RNA HELICASE DOMAIN

Released:
Primary publication:
Structure of the hepatitis C virus RNA helicase domain.
Nat Struct Biol 4 463-7 (1997)
PMID: 9187654

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:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151128 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine protease/helicase NS3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 451 amino acids
Theoretical weight: 48.36 KDa
Source organism: Hepatitis C virus (isolate 1)
Expression system: Escherichia coli
UniProt:
  • Canonical: P27958 (Residues: 1206-1656; Coverage: 15%)
Sequence domains: Flavivirus DEAD domain
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 81.54Å b: 102.73Å c: 119.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.32
Expression system: Escherichia coli