5fgb

X-ray diffraction
1.65Å resolution

Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC33.4

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-210948 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Anti-HCV E2 Fab HC84-1 light chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 216 amino acids
Theoretical weight: 23.51 KDa
Source organism: Homo sapiens
Expression system: Drosophila
Structure domains: Immunoglobulins
Anti-HCV E2 Fab HC84-1 heavy chain Chains: C, E
Molecule details ›
Chains: C, E
Length: 269 amino acids
Theoretical weight: 28.39 KDa
Source organism: Homo sapiens
Expression system: Drosophila
Structure domains: Immunoglobulins
Envelope glycoprotein E2 Chains: F, G
Molecule details ›
Chains: F, G
Length: 21 amino acids
Theoretical weight: 2.3 KDa
Source organism: Hepatitis C virus (isolate H)
Expression system: Not provided
UniProt:
  • Canonical: P27958 (Residues: 405-425; Coverage: 1%)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SOLEIL BEAMLINE PROXIMA 1
Spacegroup: P21
Unit cell:
a: 49.81Å b: 149.43Å c: 67.95Å
α: 90° β: 90.08° γ: 90°
R-values:
R R work R free
0.172 0.171 0.19
Expression systems:
  • Drosophila
  • Not provided