Structure of the Alzheimer's Amyloid Precursor Protein (APP) Copper Binding Domain in 'small unit cell' form, atomic resolution. Determined by X-ray diffraction at 0.85 Å resolution. Released 16 Jan 2007.
Explore 2FMA in 3D Show helices and sheets RCSB PDB PDBe
2FMA contains 1 α-helix and 4 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 134-139 | 6 | 1 |
| β-strand | 145 | 1 | 1 |
| α-helix | 147-160 | 14 | |
| β-strand | 163-174 | 12 | 1 |
| β-strand | 178-188 | 11 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Amyloid beta A4 protein precursor | A | protein | 59 | Homo sapiens | P05067 (AlphaFold model) |
>2FMA_1 Amyloid beta A4 protein precursor (chains A) EACKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPL
Structure of Alzheimer's disease amyloid precursor protein copper-binding domain at atomic resolution. Kong, G.K., Adams, J.J., Cappai, R. et al. Acta Crystallogr Sect F Struct Biol Cryst Commun (2007) 63:819-824. DOI 10.1107/S1744309107041139 · PubMed
Other PDB entries of the same protein (UniProt P05067 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 2FMA directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.