› 3pmr

X-ray diffraction
2.11Å resolution

Crystal Structure of E2 domain of Human Amyloid Precursor-Like Protein 1

Released:
DOI: 10.2210/pdb3pmr/pdb
PDB entry 3pmr coloured by chain, front view.
PDB entry 3pmr coloured by chain, side view.
PDB entry 3pmr 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-156407 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid beta precursor like protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 219 amino acids
Theoretical weight: 25.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P51693 (Residues: 285-499; Coverage: 35%)
Gene name: APLP1
Sequence domains: E2 domain of amyloid precursor protein
Structure domains: Amyloid precursor protein, E2 domain

Ligands and Environments

1 bound ligand:
Ligand PO4 4 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P212121
Unit cell:
a: 74.885Å b: 81.269Å c: 89.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.244
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

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

5 mentions without citation

The E2 domains of APP and APLP1 share a conserved mode of dimerization.
Lee et al. (2011)
4 more