› 3kn0

X-ray diffraction
1.9Å 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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157562 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-secretase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 395 amino acids
Theoretical weight: 44.02 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P56817 (Residues: 53-447; Coverage: 82%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

2 bound ligands:
Ligand 3TO 2 x 3TO
Ligand TLA 2 x TLA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-BM
Spacegroup: P212121
Unit cell:
a: 86.448Å b: 89.741Å c: 131.265Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.222
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Function, therapeutic potential and cell biology of BACE proteases: current status and future prospects.
Vassar et al. (2014)
11 more

2 mentions without citation

Fragment-based Binding Efficiency Indices in Bioactive Molecular Design: A Computational Approach to BACE-1 Inhibitors.
Razzaghi-Asl et al. (2013)
1 more