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X-ray diffraction
2.4Å resolution

Structure of the core ectodomain of the hepatitis C virus envelope glycoprotein 2

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:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Core protein precursor Chain: E
Molecule details ›
Chain: E
Length: 217 amino acids
Theoretical weight: 24.27 KDa
Source organism: Hepatitis C virus subtype 2a
Expression system: Lentivirus
UniProt:
  • Canonical: Q9QF35 (Residues: 456-655; Coverage: 7%)
Mouse Fab Heavy Chain Chain: H
Molecule details ›
Chain: H
Length: 467 amino acids
Theoretical weight: 51.34 KDa
Source organism: Mus musculus
Expression system: Lentivirus
Structure domains: Immunoglobulins
Mouse Fab Light Chain Chain: L
Molecule details ›
Chain: L
Length: 240 amino acids
Theoretical weight: 26.55 KDa
Source organism: Mus musculus
Expression system: Lentivirus
Structure domains: Immunoglobulins

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P21212
Unit cell:
a: 85.96Å b: 194.57Å c: 37.92Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.199 0.259
Expression system: Lentivirus