› 3zks

X-ray diffraction
2.11Å resolution

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:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-212883 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-secretase 2 Chain: A
Molecule details ›
Chain: A
Length: 386 amino acids
Theoretical weight: 42.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y5Z0 (Residues: 75-460; Coverage: 78%)
Gene names: AEPLC, ALP56, ASP21, BACE2, CDA13, UNQ418/PRO852
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases
XA4813 Chain: D
Molecule details ›
Chain: D
Length: 122 amino acids
Theoretical weight: 13.15 KDa
Source organism: Lama glama
Expression system: Escherichia coli
Structure domains: Immunoglobulins

Ligands and Environments

1 bound ligand:
Ligand WZV 1 x WZV
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P212121
Unit cell:
a: 64.101Å b: 74.764Å c: 108.721Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.211 0.208 0.26
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli

Quick links

Citations

5 review citations

Nanobodies as Probes for Protein Dynamics in Vitro and in Cells.
Dmitriev et al. (2016)
4 more

1 mention without citation

A Structure-Based Discovery Platform for BACE2 and the Development of Selective BACE Inhibitors.
Yen et al. (2021)