› 2qk5

X-ray diffraction
2.2Å resolution

Structure of BACE1 bound to SCH626485

Released:
DOI: 10.2210/pdb2qk5/pdb
PDB entry 2qk5 coloured by chain, front view.
PDB entry 2qk5 coloured by chain, side view.
PDB entry 2qk5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Potent pyrrolidine- and piperidine-based BACE-1 inhibitors.
Iserloh U, Wu Y, Cumming JN, Pan J, Wang LY, Stamford AW, Kennedy ME, Kuvelkar R, Chen X, Parker EM, Strickland C, Voigt J
Bioorg Med Chem Lett 18 414-7 (2008)
PMID: 18023580

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 domain:

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 395 amino acids
Theoretical weight: 43.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P56817 (Residues: 55-447; Coverage: 82%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

1 bound ligand:
Ligand CS5 2 x CS5
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 86.485Å b: 89.204Å c: 131.147Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.19 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Developing β-secretase inhibitors for treatment of Alzheimer's disease.
Ghosh et al. (2012)
3 more

5 mentions without citation

Exploring the binding of BACE-1 inhibitors using comparative binding energy analysis (COMBINE).
Liu et al. (2012)
4 more