2f55

X-ray diffraction
3.3Å resolution

Two hepatitis c virus ns3 helicase domains complexed with the same strand of dna

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

Assemblies composition:
hetero trimer (preferred)
hetero dimer
PDBe Complex ID:
PDB-CPX-218914 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
Macromolecules (3 distinct):
Serine protease/helicase NS3 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 435 amino acids
Theoretical weight: 46.57 KDa
Source organism: Hepacivirus C
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O92972 (Residues: 1216-1650; Coverage: 15%)
Sequence domains: Flavivirus DEAD domain
Structure domains:
5'-D(P*(DU)P*(DU)P*(DU)P*(DU)P*(DU)P*(DU)P*(DU)P*(DU)P*(DU)P*(DU)P*(DU)P*(DU)P*(DU))-3' Chain: D
Molecule details ›
Chain: D
Length: 13 nucleotides
Theoretical weight: 3.73 KDa
Source organism: Synthetic construct
Expression system: Not provided
5'-D(P*(DU)P*(DU)P*(DU))-3' Chain: E
Molecule details ›
Chain: E
Length: 3 nucleotides
Theoretical weight: 826 Da
Source organism: Synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 108.2Å b: 109.8Å c: 183.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.247 0.273
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided