PDBe 2fma

X-ray diffraction
0.85Å resolution

Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'small unit cell' form, atomic resolution

Released:
Source organism: Homo sapiens
Primary publication:
Structure of Alzheimer's disease amyloid precursor protein copper-binding domain at atomic resolution.
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 63 819-24 (2007)
PMID: 17909280

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-APP Chain: A
Molecule details ›
Chain: A
Length: 59 amino acids
Theoretical weight: 6.85 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P05067 (Residues: 133-189; Coverage: 8%)
Gene names: A4, AD1, APP
Structure domains: Amyloid beta a4 protein copper binding domain

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 31.289Å b: 32.488Å c: 50.088Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.13 0.13 0.15
Expression system: Komagataella pastoris