PDBe 3uqu

X-ray diffraction
1.7Å resolution

Crystal structure of BACE1 with its inhibitor

Released:
Source organism: Homo sapiens
Entry authors: Chen TT, Chen WY, Xu YC

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: 433 amino acids
Theoretical weight: 48.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P56817 (Residues: 43-454; Coverage: 86%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2221
Unit cell:
a: 104.467Å b: 128.235Å c: 76.176Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.163 0.195
Expression system: Escherichia coli