› 5erw

X-ray diffraction
2.9Å resolution

Structure of HCV E2 glycoprotein antigenic Epitope II bound to the broadly neutralizing antibody HC84-26

Released:
DOI: 10.2210/pdb5erw/pdb
PDB entry 5erw coloured by chain, front view.
PDB entry 5erw coloured by chain, side view.
PDB entry 5erw coloured by chain, top view.
Source organism: Homo sapiens
Entry authors: Gao M, Mariuzza R

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
Sequence domains:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-210947 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Anti-HCV E2 Fab HC84-26 heavy chain Chain: A
Molecule details ›
Chain: A
Length: 217 amino acids
Theoretical weight: 23.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins
Anti-HCV E2 Fab HC84-26 light chain Chain: B
Molecule details ›
Chain: B
Length: 214 amino acids
Theoretical weight: 23.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
Structure domains: Immunoglobulins
Envelope glycoprotein E2 Chain: C
Molecule details ›
Chain: C
Length: 13 amino acids
Theoretical weight: 1.54 KDa
UniProt:
  • Canonical: P27958 (Residues: 434-446; Coverage: 0%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: Cu FINE FOCUS
Unit cell:
a: 37.7Å b: 101.24Å c: 180.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.215 0.258
Expression system: Escherichia coli

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