› 3uqp

X-ray diffraction
1.77Å 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-157549 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-secretase 1 Chain: A
Molecule details ›
Chain: A
Length: 433 amino acids
Theoretical weight: 48.22 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
METHYL (2R)-1-[(6S,9S,12S,13S,17S,20S,23R)-9-(3-AMINO-3-OXOPROPYL)-12,23-DIBENZYL-13-HYDROXY-2,2,8,20,22-PENTAMETHYL-17-(2-METHYLPROPYL)-4,7,10,15,18,21,24-HEPTAOXO-6-(PROPAN-2-YL)-3-OXA-5,8,11,16,19,22-HEXAAZATETRACOSAN-24-YL]PYRROLIDINE-2-CARBOXYLATE Chain: B
Molecule details ›
Chain: B
Length: 8 amino acids
Theoretical weight: 1.01 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
1 modified residue:
Ligand GNC 1 x GNC

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: C2221
Unit cell:
a: 104.39Å b: 128.06Å c: 76.17Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.166 0.165 0.189
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

13 review citations

Biological targets and mechanisms of action of natural products from marine cyanobacteria.
Salvador-Reyes et al. (2015)
12 more