› 3ifp

X-ray diffraction
2.95Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-209161 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
12B4 FAB antibody heavy chain Chains: A, C, E, H
Molecule details ›
Chains: A, C, E, H
Length: 226 amino acids
Theoretical weight: 24.59 KDa
Source organism: Mus musculus
Expression system: Cricetulus griseus
Structure domains: Immunoglobulins
12B4 FAB antibody light chain Chains: B, D, F, L
Molecule details ›
Chains: B, D, F, L
Length: 219 amino acids
Theoretical weight: 24.17 KDa
Source organism: Mus musculus
Expression system: Cricetulus griseus
Structure domains: Immunoglobulins
Amyloid-beta protein 40 Chains: P, Q, R, S
Molecule details ›
Chains: P, Q, R, S
Length: 7 amino acids
Theoretical weight: 891 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 672-678; Coverage: 1%)
Gene names: A4, AD1, APP

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P1
Unit cell:
a: 78.86Å b: 79.24Å c: 94.1Å
α: 68.66° β: 65.28° γ: 78.47°
R-values:
R R work R free
0.236 0.235 0.269
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