PDBe 3ow9

X-ray diffraction
1.8Å resolution

Structure of an amyloid forming peptide KLVFFA from amyloid beta, alternate polymorph II

Source organism: synthetic construct
Primary publication:
Molecular basis for amyloid-beta polymorphism.
Proc. Natl. Acad. Sci. U.S.A. 108 16938-43 (2011)
PMID: 21949245

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo 12-mer (preferred)
Entry contents:
1 distinct polypeptide molecule
P3(40) Chains: A, B
Molecule details ›
Chains: A, B
Length: 6 amino acids
Theoretical weight: 725 Da
Source organism: synthetic construct
Expression system: Not provided
  • Canonical: NEW P05067 (Residues: 687-692; 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: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 46.053Å b: 9.561Å c: 20.871Å
α: 90° β: 97.43° γ: 90°
R R work R free
0.213 0.208 0.258
Expression system: Not provided