5mcq

X-ray diffraction
1.82Å resolution

CRYSTAL STRUCTURE OF BACE-1 IN COMPLEX WITH ACTIVE SITE AND EXOSITE BINDING PEPTIDE INHIBITOR

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.
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-secretase 1 Chain: A
Molecule details ›
Chain: A
Length: 409 amino acids
Theoretical weight: 45.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P56817 (Residues: 46-454; Coverage: 85%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
BACE-1 ACTIVE AND EXOSITE BINDING INHIBITOR Chain: D
Molecule details ›
Chain: D
Length: 22 amino acids
Theoretical weight: 2.23 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P3221
Unit cell:
a: 101.93Å b: 101.93Å c: 116.35Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.178 0.224
Expression systems:
  • Escherichia coli
  • Not provided