› 2zht

X-ray diffraction
2.35Å resolution

Crystal structure of BACE1 at pH 4.5

Released:
DOI: 10.2210/pdb2zht/pdb
PDB entry 2zht coloured by chain, front view.
PDB entry 2zht coloured by chain, side view.
PDB entry 2zht coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of an active form of BACE1, an enzyme responsible for amyloid beta protein production.
Shimizu H, Tosaki A, Kaneko K, Hisano T, Sakurai T, Nukina N
Mol Cell Biol 28 3663-71 (2008)
PMID: 18378702

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 Chain: A
Molecule details ›
Chain: A
Length: 411 amino acids
Theoretical weight: 45.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P56817 (Residues: 45-454; Coverage: 85%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44B2
Spacegroup: P6122
Unit cell:
a: 102.594Å b: 102.594Å c: 171.159Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.197 0.244
Expression system: Escherichia coli BL21

Quick links

Citations

20 review citations

Expression and function of epithelial cell adhesion molecule EpCAM: where are we after 40 years?
Gires et al. (2020)
19 more

5 mentions without citation

Crystal structure of an active form of BACE1, an enzyme responsible for amyloid beta protein production.
Shimizu et al. (2008)
4 more