2FMA: Amyloid beta A4 protein precursor

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.

Method
X-ray diffraction
Resolution
0.85 Å
Organism
Homo sapiens
Chains
1
Atoms
613
Mol. weight
6.94 kDa
Released
16 Jan 2007

Explore 2FMA in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 1 helix, 4 β-strands

ElementResiduesLengthSheet
β-strand134-13961
β-strand14511
α-helix147-16014
β-strand163-174121
β-strand178-188111

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Amyloid beta A4 protein precursorAprotein59Homo sapiensP05067 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>2FMA_1 Amyloid beta A4 protein precursor (chains A)
EACKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPL

Primary citation

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:

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