4oow

X-ray diffraction
2.57Å resolution

HCV NS5B polymerase with a fragment of quercetagetin

Released:

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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'.
ATP + H(2)O = ADP + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 578 amino acids
Theoretical weight: 64.53 KDa
Source organism: Hepatitis C virus isolate HC-J4
Expression system: Escherichia coli
UniProt:
  • Canonical: O92972 (Residues: 2420-2989; Coverage: 19%)
Sequence domains: Viral RNA dependent RNA polymerase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 106.6Å b: 108.87Å c: 134.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.221 0.216 0.277
Expression system: Escherichia coli