4aep

X-ray diffraction
1.8Å resolution

HCV-JFH1 NS5B POLYMERASE STRUCTURE AT 1.8 ANGSTROM

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
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-189307 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-directed RNA polymerase Chain: A
Molecule details ›
Chain: A
Length: 579 amino acids
Theoretical weight: 64.63 KDa
Source organism: Hepacivirus hominis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99IB8 (Residues: 2443-3013; 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 ID14-4
Spacegroup: C2221
Unit cell:
a: 100.97Å b: 110.52Å c: 115.26Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.187 0.227
Expression system: Escherichia coli BL21(DE3)