PDBe 5f00

X-ray diffraction
1.95Å resolution

CRYSTAL STRUCTURE OF BACE-1 IN COMPLEX WITH 5-[3-[(3-chloro-8-quinolyl)amino]phenyl]-5-methyl-2,6-dihydro-1,4-oxazin-3-amine

Released:

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
Macromolecule:
Beta-secretase 1 Chain: A
Molecule details ›
Chain: A
Length: 390 amino acids
Theoretical weight: 43.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
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

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P6122
Unit cell:
a: 103.504Å b: 103.504Å c: 169.212Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.223 0.22 0.263
Expression system: Escherichia coli