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X-ray diffraction
2.05Å resolution

Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC84-1

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

Assemblies composition:
hetero dimer
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-210941 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Anti-HCV E2 Fab HC84-1 heavy chain Chains: A, C, I
Molecule details ›
Chains: A, C, I
Length: 261 amino acids
Theoretical weight: 27.55 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
Structure domains: Immunoglobulins
Anti-HCV E2 Fab HC84-1 light chain Chains: B, D, P
Molecule details ›
Chains: B, D, P
Length: 215 amino acids
Theoretical weight: 23.2 KDa
Source organism: Homo sapiens
Expression system: Drosophila melanogaster
Structure domains: Immunoglobulins
Envelope glycoprotein E2 Chain: K
Molecule details ›
Chain: K
Length: 13 amino acids
Theoretical weight: 1.54 KDa
Source organism: Hepatitis C virus (isolate H)
Expression system: Not provided
UniProt:
  • Canonical: P27958 (Residues: 434-446; Coverage: 0%)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2221
Unit cell:
a: 76.521Å b: 165.568Å c: 269.323Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.235
Expression systems:
  • Drosophila melanogaster
  • Not provided