2zhr

X-ray diffraction
2.5Å resolution

Crystal structure of BACE1 in complex with OM99-2 at pH 5.0

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)
PDBe Complex ID:
PDB-CPX-157548 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-secretase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 411 amino acids
Theoretical weight: 45.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P56817 (Residues: 45-454; Coverage: 85%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
inhibitor OM99-2 Chains: C, D
Molecule details ›
Chains: C, D
Length: 7 amino acids
Theoretical weight: 893 Da
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: SPRING-8 BEAMLINE BL26B2
Spacegroup: P212121
Unit cell:
a: 86.333Å b: 89.912Å c: 130.794Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.185 0.24
Expression systems:
  • Escherichia coli BL21
  • Not provided