› 3ckp

X-ray diffraction
2.3Å resolution

Crystal structure of BACE-1 in complex with inhibitor

Released:
DOI: 10.2210/pdb3ckp/pdb
PDB entry 3ckp coloured by chain, front view.
PDB entry 3ckp coloured by chain, side view.
PDB entry 3ckp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Synthesis, SAR, and X-ray structure of human BACE-1 inhibitors with cyclic urea derivatives.
Park H, Min K, Kwak HS, Koo KD, Lim D, Seo SW, Choi JU, Platt B, Choi DY
Bioorg Med Chem Lett 18 2900-4 (2008)
PMID: 18434152

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, C
Molecule details ›
Chains: A, B, C
Length: 412 amino acids
Theoretical weight: 45.92 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P56817 (Residues: 43-454; Coverage: 86%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

2 bound ligands:
Ligand CL 9 x CL
Ligand 012 3 x 012
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 4A
Spacegroup: C2
Unit cell:
a: 224.064Å b: 105.654Å c: 63.7Å
α: 90° β: 101.47° γ: 90°
R-values:
R R work R free
0.245 0.245 0.304
Expression system: Escherichia coli

Quick links

Citations

1 review citation

BACE-1 and γ-Secretase as Therapeutic Targets for Alzheimer's Disease.
Maia et al. (2019)
5 other articles

1 mention without citation

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