4wti

X-ray diffraction
2.8Å resolution

CRYSTAL STRUCTURE OF HCV NS5B GENOTYPE 2A JFH-1 ISOLATE WITH S15G E86Q E87Q C223H V321I MUTATIONS IN COMPLEX WITH RNA TEMPLATE 5'-ACGG, RNA PRIMER 5'-PCC, MN2+, AND GDP

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:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct RNA molecules
Macromolecules (3 distinct):
RNA-directed RNA polymerase Chain: A
Molecule details ›
Chain: A
Length: 580 amino acids
Theoretical weight: 64.82 KDa
Source organism: Hepatitis C virus JFH-1
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q99IB8 (Residues: 2443-3012; Coverage: 19%)
Sequence domains: Viral RNA dependent RNA polymerase
RNA TEMPLATE ACGG Chain: T
Molecule details ›
Chain: T
Length: 4 nucleotides
Theoretical weight: 1.28 KDa
Source organism: synthetic construct
Expression system: Not provided
RNA PRIMER CC Chain: P
Molecule details ›
Chain: P
Length: 2 nucleotides
Theoretical weight: 565 Da
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P65
Unit cell:
a: 140.15Å b: 140.15Å c: 92.76Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.184 0.181 0.234
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided