› 4l7g

X-ray diffraction
1.38Å resolution

Diethylaminosulfur Trifluoride-Mediated Intramolecular Cyclization of 2-hydroxy-benzylureas to Fused Bicyclic Aminooxazoline Compounds and Evaluation of Their Biochemical Activity Against Beta-Secretase-1 (BACE1)

Released:
DOI: 10.2210/pdb4l7g/pdb
PDB entry 4l7g coloured by chain, front view.
PDB entry 4l7g coloured by chain, side view.
PDB entry 4l7g coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Diethylaminosulfur Trifluoride-Mediated Intramolecular Cyclization of 2-hydroxycycloalkylureas to Fused Bicyclic Aminooxazoline Compounds and Evaluation of Their Biochemical Activity Against β-Secretase-1 (BACE-1)
Huestis MP, Liu W, Volgraf M, Purkey H, Yu C, Wang W, Smith D, Vigers G, Dutcher D, Hunt KW, Siu M
Tetrahedron Lett. (2013)

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:
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: 409 amino acids
Theoretical weight: 45.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P56817 (Residues: 57-453; Coverage: 83%)
Gene names: BACE, BACE1, KIAA1149
Sequence domains: Eukaryotic aspartyl protease
Structure domains: Acid Proteases

Ligands and Environments

2 bound ligands:
Ligand 1W0 1 x 1W0
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: C2
Unit cell:
a: 72.664Å b: 104.471Å c: 50.076Å
α: 90° β: 94.82° γ: 90°
R-values:
R R work R free
0.156 0.154 0.192
Expression system: Escherichia coli

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