2y3k

X-ray diffraction
1.9Å resolution

Structure of segment MVGGVVIA from the amyloid-beta peptide (Ab, residues 35-42), alternate polymorph 1

Released:
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 dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
P3(40) Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 8 amino acids
Theoretical weight: 745 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • 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: P1
Unit cell:
a: 9.47Å b: 20.28Å c: 47.69Å
α: 90.21° β: 89.78° γ: 103.55°
R-values:
R R work R free
0.214 0.214 0.231
Expression system: Not provided