PDBe 2zji

X-ray diffraction
2.3Å resolution

Crystal structure of the human BACE1 catalytic domain in complex with N-[1-(2,6-dimethoxy-benzyl)-piperidin-4-yl]-4-mercapto-butyramide

Released:
Source organism: Homo sapiens
Entry authors: Randal M, Lam MB, Romanowski MJ

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: 405 amino acids
Theoretical weight: 45.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P56817 (Residues: 43-446; Coverage: 84%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P6122
Unit cell:
a: 103.306Å b: 103.306Å c: 168.014Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.236 0.234 0.264
Expression system: Escherichia coli