› 4i0e

X-ray diffraction
1.7Å resolution

Design and Synthesis of Thiophene Dihydroisoquinolins as Novel BACE-1 Inhibitors

Released:
DOI: 10.2210/pdb4i0e/pdb
PDB entry 4i0e coloured by chain, front view.
PDB entry 4i0e coloured by chain, side view.
PDB entry 4i0e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Design and synthesis of thiophene dihydroisoquinolines as novel BACE1 inhibitors.
Xu YZ, Yuan S, Bowers S, Hom RK, Chan W, Sham HL, Zhu YL, Beroza P, Pan H, Brecht E, Yao N, Lougheed J, Yan J, Tam D, Ren Z, Ruslim L, Bova MP, Artis DR
Bioorg Med Chem Lett 23 3075-80 (2013)
PMID: 23570791

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

Assemblies composition:
monomeric (preferred)
homo dimer
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: 406 amino acids
Theoretical weight: 45.45 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P56817 (Residues: 57-453; Coverage: 83%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

2 bound ligands:
Ligand ZN 3 x ZN
Ligand 1B8 1 x 1B8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: C2221
Unit cell:
a: 75.062Å b: 103.335Å c: 100.306Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.23 0.3
Expression system: Not provided

Quick links

Citations

1 review citation

Development and Structural Modification of BACE1 Inhibitors.
Gu et al. (2016)
4 other articles