› 4dpf

X-ray diffraction
1.8Å resolution

Function and Biology Details

Reaction catalysed: 
Broad endopeptidase specificity. Cleaves Glu-Val-Asn-Leu-|-Asp-Ala-Glu-Phe in the Swedish variant of Alzheimer's amyloid precursor protein.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157541 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-secretase 1 Chain: A
Molecule details ›
Chain: A
Length: 391 amino acids
Theoretical weight: 43.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P56817 (Residues: 57-446; Coverage: 81%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand 0LG 1 x 0LG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P212121
Unit cell:
a: 47.76Å b: 76.71Å c: 103.88Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.192 0.239
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The structural evolution of β-secretase inhibitors: a focus on the development of small-molecule inhibitors.
Butini et al. (2013)
7 other articles

16 mentions without citation

Afferent Connectivity of the Zebrafish Habenulae.
Turner et al. (2016)
15 more