6bzw

X-ray diffraction
2.2Å resolution

Structure of the Hepatitis C virus envelope glycoprotein E2 antigenic region 412-423 bound to the GL precursor of the broadly neutralizing antibody AP33

Released:

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-230918 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
AP33 GL Heavy Chain Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
Length: 223 amino acids
Theoretical weight: 23.99 KDa
Source organism: Mus musculus
Expression system: Homo sapiens
AP33 GL Light Chain Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 219 amino acids
Theoretical weight: 23.85 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
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: 60.356Å b: 84.709Å c: 192.919Å
α: 90° β: 89.96° γ: 90°
R-values:
R R work R free
0.213 0.192 0.231
Expression system: Homo sapiens