4gaj

X-ray diffraction
2.51Å resolution

Structure of the broadly neutralizing antibody AP33 in complex with its HCV epitope (E2 residues 411-424)

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
NEUTRALIZING ANTIBODY AP33 HEAVY CHAIN Chain: H
Molecule details ›
Chain: H
Length: 218 amino acids
Theoretical weight: 23.68 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
NEUTRALIZING ANTIBODY AP33 LIGHT CHAIN Chain: L
Molecule details ›
Chain: L
Length: 218 amino acids
Theoretical weight: 23.92 KDa
Source organism: Mus musculus
Structure domains: Immunoglobulins
Genome polyprotein Chain: P
Molecule details ›
Chain: P
Length: 14 amino acids
Theoretical weight: 1.67 KDa
Source organism: Hepacivirus C
Expression system: Not provided
UniProt:
  • Canonical: Q9IY15 (Residues: 94-107; Coverage: 8%)

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2
Unit cell:
a: 171.91Å b: 40.67Å c: 73.77Å
α: 90° β: 112.11° γ: 90°
R-values:
R R work R free
0.244 0.24 0.32
Expression system: Not provided