› 6fgy

X-ray diffraction
1.54Å resolution

Crystal Structure of Human BACE-1 in Complex with amino-1,4-oxazine compound 4

Released:
DOI: 10.2210/pdb6fgy/pdb
PDB entry 6fgy coloured by chain, front view.
PDB entry 6fgy coloured by chain, side view.
PDB entry 6fgy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of amino-1,4-oxazines as potent BACE-1 inhibitors.
Veenstra SJ, Rueeger H, Voegtle M, Lueoend R, Holzer P, Hurth K, Tintelnot-Blomley M, Frederiksen M, Rondeau JM, Jacobson L, Staufenbiel M, Neumann U, Machauer R
Bioorg Med Chem Lett 28 2195-2200 (2018)
PMID: 29764741

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:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-157541 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-secretase 1 Chain: A
Molecule details ›
Chain: A
Length: 396 amino acids
Theoretical weight: 44.09 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P56817 (Residues: 60-453; Coverage: 82%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand D9W 1 x D9W
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 48.056Å b: 76.738Å c: 104.214Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.204 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The β-secretase (BACE) inhibitor NB-360 in preclinical models: From amyloid-β reduction to downstream disease-relevant effects.
Neumann et al. (2019)

1 mention without citation

Partial Characterization of Two Cathepsin D Family Aspartic Peptidases of Clonorchis sinensis.
Kang et al. (2019)