1xn3

X-ray diffraction
2Å resolution

Crystal structure of Beta-secretase bound to a long inhibitor with additional upstream residues.

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

Assemblies composition:
monomeric
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-157545 (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
Peptidic inhibitor Chain: I
Molecule details ›
Chain: I
Length: 14 amino acids
Theoretical weight: 1.65 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: RIGAKU RU300
Spacegroup: P21
Unit cell:
a: 86.164Å b: 130.874Å c: 88.574Å
α: 90° β: 97.27° γ: 90°
R-values:
R R work R free
0.202 not available 0.237
Expression systems:
  • Escherichia coli BL21
  • Not provided