› 4rd9

X-ray diffraction
2.6Å resolution

X-RAY STRUCTURE OF THE APO FORM OF THE AMYLOID PRECURSOR PROTEIN-LIKE PROTEIN 1 (APLP1) E2 DOMAIN

Released:
DOI: 10.2210/pdb4rd9/pdb
PDB entry 4rd9 coloured by chain, front view.
PDB entry 4rd9 coloured by chain, side view.
PDB entry 4rd9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Interaction of the amyloid precursor protein-like protein 1 (APLP1) E2 domain with heparan sulfate involves two distinct binding modes.
Dahms SO, Mayer MC, Roeser D, Multhaup G, Than ME
OpenAccess logo Acta Crystallogr D Biol Crystallogr 71 494-504 (2015)
PMID: 25760599

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-546751 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid beta precursor like protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 203 amino acids
Theoretical weight: 23.67 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P51693 (Residues: 292-494; Coverage: 33%)
Gene name: APLP1
Sequence domains: E2 domain of amyloid precursor protein
Structure domains: Amyloid precursor protein, E2 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P212121
Unit cell:
a: 66.425Å b: 79.145Å c: 95.201Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.215 0.247
Expression system: Komagataella pastoris

Quick links

Citations

3 review citations

Restoring Soluble Amyloid Precursor Protein α Functions as a Potential Treatment for Alzheimer's Disease.
Habib et al. (2017)
2 more

1 mention without citation

Interaction of the amyloid precursor protein-like protein 1 (APLP1) E2 domain with heparan sulfate involves two distinct binding modes.
Dahms et al. (2015)