4dgy

X-ray diffraction
1.8Å resolution

Structure of the Hepatitis C virus envelope glycoprotein E2 antigenic region 412-423 bound to the broadly neutralizing antibody HCV1, C2 form

Released:
Source organism: Homo sapiens

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-541327 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
HCV1 Heavy Chain Chain: H
Molecule details ›
Chain: H
Length: 226 amino acids
Theoretical weight: 24.58 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins
HCV1 Light Chain Chain: L
Molecule details ›
Chain: L
Length: 213 amino acids
Theoretical weight: 23.4 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Structure domains: Immunoglobulins
Envelope glycoprotein E2 Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.55 KDa
UniProt:
  • Canonical: P26663 (Residues: 412-423; Coverage: 0%)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2
Unit cell:
a: 141.099Å b: 63.065Å c: 69.3Å
α: 90° β: 95.72° γ: 90°
R-values:
R R work R free
0.189 0.188 0.221
Expression system: Homo sapiens