8ohm

X-ray diffraction
2.3Å resolution

CRYSTAL STRUCTURE OF RNA HELICASE FROM GENOTYPE 1B HEPATITIS C VIRUS: MECHANISM OF UNWINDING DUPLEX RNA

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:
Biological process:
  • not assigned
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 Chain: A
Molecule details ›
Chain: A
Length: 435 amino acids
Theoretical weight: 46.6 KDa
Source organism: Hepacivirus hominis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P26663 (Residues: 1216-1650; Coverage: 15%)
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE M18X
Spacegroup: P3121
Unit cell:
a: 93.3Å b: 93.3Å c: 104.6Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.233 0.303
Expression system: Escherichia coli BL21(DE3)