5fgc

X-ray diffraction
1.9Å resolution

Three dimensional structure of broadly neutralizing human anti - Hepatitis C virus (HCV) glycoprotein E2 Fab fragment HC33.8

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-210949 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Envelope glycoprotein E2 Chain: A
Molecule details ›
Chain: A
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%)
Anti-HCV E2 Fab HC33.8 light chain Chain: B
Molecule details ›
Chain: B
Length: 216 amino acids
Theoretical weight: 23.51 KDa
Source organism: Homo sapiens
Expression system: Drosophila
Structure domains: Immunoglobulins
Anti-HCV E2 Fab HC33.8 heavy chain Chain: E
Molecule details ›
Chain: E
Length: 269 amino acids
Theoretical weight: 28.64 KDa
Source organism: Homo sapiens
Expression system: Drosophila
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P2
Unit cell:
a: 66.05Å b: 49.57Å c: 66.39Å
α: 90° β: 98.5° γ: 90°
R-values:
R R work R free
0.196 0.194 0.236
Expression systems:
  • Not provided
  • Drosophila