PDBe 4fsl

X-ray diffraction
2.5Å resolution

Crystal structure of beta-site app-cleaving enzyme 1 (BACE-DB-MUT) complex with N-(N-(4- acetamido-3-chloro-5-methylbenzyl)carbamimidoyl)-3-(4- methoxyphenyl)-5-methyl-4-isothiazolecarboxamide


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. 
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Beta-secretase 1 Chains: A, B, D, E
Molecule details ›
Chains: A, B, D, E
Length: 412 amino acids
Theoretical weight: 45.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: P56817 (Residues: 43-453; Coverage: 86%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 86.54Å b: 131.177Å c: 90.315Å
α: 90° β: 97.61° γ: 90°
R R work R free
0.226 0.224 0.277
Expression system: Escherichia coli BL21(DE3)