PDBe 2zjo

X-ray diffraction
2.5Å resolution

Crystal structure of hepatitis C virus NS3 helicase with a novel inhibitor

Released:
Entry authors: Liaw SH, Chen SJ, Hu CY, Chi WK, Chu ID, Hwang LH, Chern JW, Chen DS

Function and Biology Details

Reactions catalysed:
ATP + H(2)O = ADP + phosphate. 
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'. 
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). 
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 NS3 Chain: A
Molecule details ›
Chain: A
Length: 482 amino acids
Theoretical weight: 51.88 KDa
Source organism: Hepatitis C virus (isolate Taiwan)
Expression system: Escherichia coli
UniProt:
  • Canonical: P29846 (Residues: 1193-1657; 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: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: P3121
Unit cell:
a: 92.063Å b: 92.063Å c: 104.71Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.23 0.23 0.287
Expression system: Escherichia coli