PDBe 1xn2

X-ray diffraction
1.9Å resolution

New substrate binding pockets for beta-secretase.

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-secretase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 389 amino acids
Theoretical weight: 43.31 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P56817 (Residues: 58-446; Coverage: 81%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
OM03-4 Chains: E, F, G, H
Molecule details ›
Chains: E, F, G, H
Length: 12 amino acids
Theoretical weight: 1.64 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P21
Unit cell:
a: 86.223Å b: 130.784Å c: 88.744Å
α: 90° β: 97.71° γ: 90°
R-values:
R R work R free
0.193 not available 0.22
Expression systems:
  • Escherichia coli BL21
  • Not provided