Solution NMR

Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode


Function and Biology Details

Structure analysis Details

Assembly composition:
Non-polymer only dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
C31 Chain: A
Molecule details ›
Chain: A
Length: 32 amino acids
Theoretical weight: 3.84 KDa
Source organism: Mus musculus
Expression system: Not provided
  • Canonical: P12023 (Residues: 739-770; Coverage: 4%)
Gene name: App
Amyloid-beta A4 precursor protein-binding family B member 2 Chain: B
Molecule details ›
Chain: B
Length: 136 amino acids
Theoretical weight: 14.75 KDa
Source organism: Mus musculus
Expression system: CELL-FREE SYNTHESIS
  • Canonical: Q9DBR4 (Residues: 582-704; Coverage: 16%)
Gene name: Apbb2
Structure domains: Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Chemical shifts: BMR10236  
Expression system: CELL-FREE SYNTHESIS