› 3ifn

X-ray diffraction
1.5Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-209159 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
12A11 FAB antibody heavy chain Chain: H
Molecule details ›
Chain: H
Length: 222 amino acids
Theoretical weight: 23.98 KDa
Source organism: Mus musculus
Expression system: Cricetulus griseus
Structure domains: Immunoglobulins
12A11 FAB antibody light chain Chain: L
Molecule details ›
Chain: L
Length: 219 amino acids
Theoretical weight: 24.09 KDa
Source organism: Mus musculus
Expression system: Cricetulus griseus
Structure domains: Immunoglobulins
Amyloid-beta protein 40 Chain: P
Molecule details ›
Chain: P
Length: 40 amino acids
Theoretical weight: 4.34 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 672-711; Coverage: 5%)
Gene names: A4, AD1, APP
Sequence domains: Beta-amyloid peptide (beta-APP)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 42.99Å b: 87.01Å c: 58.99Å
α: 90° β: 95.77° γ: 90°
R-values:
R R work R free
0.188 0.187 0.212
Expression systems:
  • Cricetulus griseus
  • Not provided

Quick links

Citations

3 review citations

On the subject of rigor in the study of amyloid β-protein assembly.
Teplow DB. (2013)
2 more

5 mentions without citation

Conformational selection in amyloid-based immunotherapy: Survey of crystal structures of antibody-amyloid complexes.
Ma et al. (2016)
4 more