3kqn

X-ray diffraction
2.05Å resolution

Three Conformational Snapshots of the Hepatitis C Virus NS3 Helicase Reveal a Ratchet Translocation Mechanism

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:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-116501 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Serine protease/helicase NS3 Chain: A
Molecule details ›
Chain: A
Length: 437 amino acids
Theoretical weight: 46.74 KDa
Source organism: Hepatitis C virus (isolate Con1)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9WMX2 (Residues: 1215-1650; Coverage: 15%)
Sequence domains: Flavivirus DEAD domain
Structure domains:
5'-D(*TP*TP*TP*TP*TP*T)-3' Chain: E
Molecule details ›
Chain: E
Length: 6 nucleotides
Theoretical weight: 1.78 KDa
Source organism: Hepatitis C virus (isolate Con1)
Expression system: Not provided

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P61
Unit cell:
a: 116.764Å b: 116.764Å c: 71.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.19 0.19 0.223
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided