X-ray diffraction
2.1Å resolution

Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42), alternate polymorph 2

Source organism: Homo sapiens
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 tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
P3(40) Chains: A, B, C, G
Molecule details ›
Chains: A, B, C, G
Length: 8 amino acids
Theoretical weight: 745 Da
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: P05067 (Residues: 706-713; 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: P21
Unit cell:
a: 9.47Å b: 47.59Å c: 20.8Å
α: 90° β: 103.57° γ: 90°
R R work R free
0.204 0.202 0.247
Expression system: Not provided