› 3nyj

X-ray diffraction
3.2Å resolution

Crystal Structure Analysis of APP E2 domain

Released:
DOI: 10.2210/pdb3nyj/pdb
PDB entry 3nyj coloured by chain, front view.
PDB entry 3nyj coloured by chain, side view.
PDB entry 3nyj coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The E2 domains of APP and APLP1 share a conserved mode of dimerization.
Lee S, Xue Y, Hu J, Wang Y, Liu X, Demeler B, Ha Y
Biochemistry 50 5453-64 (2011)
PMID: 21574595

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138395 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Soluble APP-beta Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 24.77 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05067 (Residues: 365-567; Coverage: 27%)
Gene names: A4, AD1, APP
Sequence domains: E2 domain of amyloid precursor protein
Structure domains: Amyloid precursor protein, E2 domain

Ligands and Environments

1 bound ligand:
Ligand OS 1 x OS
1 modified residue:
Ligand MSE 9 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P21212
Unit cell:
a: 114.979Å b: 40.149Å c: 58.376Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.306 0.297 0.38
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Demystifying heparan sulfate-protein interactions.
Xu et al. (2014)
4 more

3 mentions without citation

Structure and Synaptic Function of Metal Binding to the Amyloid Precursor Protein and its Proteolytic Fragments.
Wild et al. (2017)
2 more