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
Assemblies composition:
Assembly name:
PDBe Complex ID:
PDB-CPX-157560 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
ADP-ribosylation factor-binding protein GGA1
Molecule details ›
Chains: A, B
Length: 147 amino acids
Theoretical weight: 16.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: VHS domain
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Length: 147 amino acids
Theoretical weight: 16.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q9UJY5 (Residues: 1-147; Coverage: 23%)
Sequence domains: VHS domain
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Beta-secretase 1
Molecule details ›
Chain: C
Length: 12 amino acids
Theoretical weight: 1.39 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Length: 12 amino acids
Theoretical weight: 1.39 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: P56817 (Residues: 490-501; Coverage: 3%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup:
I4
Expression systems:
- Escherichia coli BL21
- Not provided
