4xvj

X-ray diffraction
2Å resolution

STRUCTURE OF THE HEPATITIS C VIRUS ENVELOPE GLYCOPROTEIN E2 ANTIGENIC 2 REGION 412-423 BOUND TO THE BROADLY NEUTRALIZING ANTIBODY HC33.1

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-210945 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Envelope glycoprotein E2 Chain: A
Molecule details ›
Chain: A
Length: 13 amino acids
Theoretical weight: 1.55 KDa
UniProt:
  • Canonical: P27958 (Residues: 412-423; Coverage: 0%)
antibody heavy chain variable domain Chain: H
Molecule details ›
Chain: H
Length: 141 amino acids
Theoretical weight: 14.88 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins
antibody light chain variable domain Chain: L
Molecule details ›
Chain: L
Length: 115 amino acids
Theoretical weight: 11.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SIEMENS
Spacegroup: P212121
Unit cell:
a: 36.085Å b: 53.728Å c: 107.238Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.225 0.225 0.274
Expression system: Escherichia coli