› 5hoy

X-ray diffraction
2.3Å resolution

X-ray crystallographic structure of an A-beta 17_36 beta-hairpin. X-ray diffractometer data set. (LVFFAEDCGSNKCAII(SAR)LMV).

Released:
DOI: 10.2210/pdb5hoy/pdb
PDB entry 5hoy coloured by chain, front view.
PDB entry 5hoy coloured by chain, side view.
PDB entry 5hoy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
X-ray Crystallographic Structures of a Trimer, Dodecamer, and Annular Pore Formed by an Aβ17-36 β-Hairpin.
Kreutzer AG, Hamza IL, Spencer RK, Nowick JS
OpenAccess logo J Am Chem Soc 138 4634-42 (2016)
PMID: 26967810

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dodecamer
homo trimer (preferred)
homo hexamer
Assembly name:
PDBe Complex ID:
PDB-CPX-529013 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
P3(40) Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 21 amino acids
Theoretical weight: 2.26 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 688-707; Coverage: 3%)
Gene names: A4, AD1, APP
Sequence domains: Beta-amyloid peptide (beta-APP)

Ligands and Environments

1 bound ligand:
Ligand JEF 1 x JEF
2 modified residues:
Ligand ORN 6 x ORN
Ligand SAR 6 x SAR

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P6122
Unit cell:
a: 97.649Å b: 97.649Å c: 97.781Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.248 0.245 0.276
Expression system: Not provided

Quick links

Citations

7 review citations

Peptide-Based Vaccines: Current Progress and Future Challenges.
Malonis et al. (2020)
6 more

4 mentions without citation

Structural Studies Providing Insights into Production and Conformational Behavior of Amyloid-β Peptide Associated with Alzheimer's Disease Development.
Urban et al. (2021)
3 more