› 3lpj

X-ray diffraction
1.79Å 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

Assemblies composition:
homo dimer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157541 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-secretase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 455 amino acids
Theoretical weight: 50.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P56817 (Residues: 14-454; Coverage: 90%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

2 bound ligands:
Ligand TLA 2 x TLA
Ligand Z75 2 x Z75
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 86.333Å b: 89.046Å c: 130.889Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.179 0.179 0.208
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Developing β-secretase inhibitors for treatment of Alzheimer's disease.
Ghosh et al. (2012)
5 more

2 mentions without citation

Structure-based predictions of activity cliffs.
Husby et al. (2015)
1 more