6bzu

X-ray diffraction
2.7Å resolution

Structure of the Hepatitis C virus envelope glycoprotein E2 antigenic region 412-423 bound to the broadly neutralizing antibody 19B3

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):
19B3 Heavy Chain Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 223 amino acids
Theoretical weight: 23.89 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
19B3 Light Chain Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 219 amino acids
Theoretical weight: 23.78 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
Structure domains: Immunoglobulins
Envelope glycoprotein E2 Chains: I, J, K, L
Molecule details ›
Chains: I, J, K, L
Length: 13 amino acids
Theoretical weight: 1.55 KDa
Source organism: Hepacivirus C
Expression system: Not provided
UniProt:
  • Canonical: P27958 (Residues: 412-423; Coverage: 0%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 132.696Å b: 55.6Å c: 155.259Å
α: 90° β: 106.2° γ: 90°
R-values:
R R work R free
0.266 0.265 0.29
Expression systems:
  • Homo sapiens
  • Not provided