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X-ray diffraction
1.9Å resolution

Structure of Hepatitis C Virus Envelope Glycoprotein E2mc3-v1 redesigned core from genotype 1a bound to broadly neutralizing antibody AR3C

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-231791 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (4 distinct):
Envelope glycoprotein E2 Chains: E, F
Molecule details ›
Chains: E, F
Length: 177 amino acids
Theoretical weight: 19.5 KDa
Source organism: Hepatitis C virus (isolate H)
Expression system: Homo sapiens
UniProt:
  • Canonical: P27958 (Residues: 412-645; Coverage: 6%)
Sequence domains: Hepatitis C virus non-structural protein E2/NS1
Fab AR3C heavy chain Chains: A, H
Molecule details ›
Chains: A, H
Length: 233 amino acids
Theoretical weight: 24.63 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
Fab AR3C light chain Chains: B, L
Molecule details ›
Chains: B, L
Length: 214 amino acids
Theoretical weight: 23.27 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-B
Spacegroup: P21
Unit cell:
a: 88.492Å b: 93.655Å c: 96.799Å
α: 90° β: 100.48° γ: 90°
R-values:
R R work R free
0.21 0.208 0.243
Expression system: Homo sapiens