› 3ktm

X-ray diffraction
2.7Å resolution

Structure of the Heparin-induced E1-Dimer of the Amyloid Precursor Protein (APP)

Released:
DOI: 10.2210/pdb3ktm/pdb
PDB entry 3ktm coloured by chain, front view.
PDB entry 3ktm coloured by chain, side view.
PDB entry 3ktm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein.
Dahms SO, Hoefgen S, Roeser D, Schlott B, Gührs KH, Than ME
Proc Natl Acad Sci U S A 107 5381-6 (2010)
PMID: 20212142

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-APP Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 191 amino acids
Theoretical weight: 21.76 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P05067 (Residues: 18-190; Coverage: 23%)
Gene names: A4, AD1, APP
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand BU4 8 x BU4
Ligand SO4 5 x SO4
Ligand ACT 4 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: R3
Unit cell:
a: 143.99Å b: 143.99Å c: 351.19Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.215 0.25
Expression system: Escherichia coli

Quick links

Citations

16 review citations

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

16 mentions without citation

Insights into the physiological function of the β-amyloid precursor protein: beyond Alzheimer's disease.
Dawkins et al. (2014)
15 more