› 2y29

X-ray diffraction
2.3Å resolution

Structure of segment KLVFFA from the amyloid-beta peptide (Ab, residues 16-21), alternate polymorph III

Released:
DOI: 10.2210/pdb2y29/pdb
PDB entry 2y29 coloured by chain, front view.
PDB entry 2y29 coloured by chain, side view.
PDB entry 2y29 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular basis for amyloid-beta polymorphism.
Colletier JP, Laganowsky A, Landau M, Zhao M, Soriaga AB, Goldschmidt L, Flot D, Cascio D, Sawaya MR, Eisenberg D
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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
P3(40) Chain: A
Molecule details ›
Chain: A
Length: 6 amino acids
Theoretical weight: 725 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: 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: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 9.59Å b: 12.07Å c: 42.21Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.224 0.26
Expression system: Not provided

Quick links

Citations

40 review citations

The amyloid state of proteins in human diseases.
Eisenberg et al. (2012)
39 more

8 mentions without citation

Molecular basis for amyloid-beta polymorphism.
Colletier et al. (2011)
7 more