› 3uqr

X-ray diffraction
3.06Å 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-157550 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Beta-secretase 1 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 433 amino acids
Theoretical weight: 48.34 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 (2S)-1-[(2R,5S,8S,12S,13S)-2,13-DIBENZYL-12-HYDROXY-3,5-DIMETHYL-15-(3-[METHYL(METHYLSULFONYL)AMINO]-5-{[(1R)-1-PHENYLETHYL]CARBAMOYL}PHENYL)-8-(2-METHYLPROPYL)-4,7,10,15-TETRAOXO-3,6,9,14-TETRAAZAPENTADECAN-1-OYL]PYRROLIDINE-2-CARBOXYLATE Chains: D, E, F
Molecule details ›
Chains: D, E, F
Length: 7 amino acids
Theoretical weight: 1.02 KDa
Source organism: synthetic construct
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PLJ 3 x PLJ

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 107.514Å b: 132.121Å c: 163.393Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.192 0.242
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