› 5i3v

X-ray diffraction
1.62Å resolution

Crystal structure of BACE1 in complex with aminoquinoline compound 1

Released:
DOI: 10.2210/pdb5i3v/pdb
PDB entry 5i3v coloured by chain, front view.
PDB entry 5i3v coloured by chain, side view.
PDB entry 5i3v coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Fragment-Linking Approach Using (19)F NMR Spectroscopy To Obtain Highly Potent and Selective Inhibitors of β-Secretase.
Jordan JB, Whittington DA, Bartberger MD, Sickmier EA, Chen K, Cheng Y, Judd T
J Med Chem 59 3732-49 (2016)
PMID: 26978477

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: 411 amino acids
Theoretical weight: 45.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P56817 (Residues: 43-453; Coverage: 86%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

3 bound ligands:
Ligand IOD 3 x IOD
Ligand 68M 1 x 68M
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P6122
Unit cell:
a: 102.953Å b: 102.953Å c: 170.381Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.21 0.209 0.231
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Highlights in BACE1 Inhibitors for Alzheimer's Disease Treatment.
Coimbra et al. (2018)
8 more