4wtg

X-ray diffraction
2.9Å resolution

CRYSTAL STRUCTURE OF HCV NS5B GENOTYPE 2A JFH-1 ISOLATE WITH S15G E86Q E87Q C223H V321I MUTATIONS AND DELTA8 BETA HAIRPIN LOOP DELETION IN COMPLEX WITH SOFOSBUVIR DIPHOSPHATE GS-607596, MN2+ AND SYMMETRICAL PRIMER TEMPLATE 5'-CAAAAUUU

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'.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct RNA molecule
Macromolecules (2 distinct):
RNA-directed RNA polymerase Chain: A
Molecule details ›
Chain: A
Length: 572 amino acids
Theoretical weight: 63.76 KDa
Source organism: Hepatitis C virus JFH-1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99IB8 (Residues: 2443-2885, 2896-3012; Coverage: 19%)
Sequence domains: Viral RNA dependent RNA polymerase
RNA PRIMER TEMPLATE CAAAAUUU Chains: P, T
Molecule details ›
Chains: P, T
Length: 8 nucleotides
Theoretical weight: 2.5 KDa

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P65
Unit cell:
a: 140.44Å b: 140.44Å c: 91.62Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.181 0.179 0.232
Expression system: Escherichia coli BL21(DE3)