6O4J: Amyloid-beta precursor protein

Amyloid Beta KLVFFAENVGS 16-26 D23N Iowa mutation. Determined by electron crystallography at 1.4 Å resolution. Released 30 Oct 2019.

Method
Electron crystallography
Resolution
1.4 Å
Organism
Homo sapiens
Chains
2
Atoms
178
Mol. weight
2.47 kDa
Released
30 Oct 2019

Explore 6O4J in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6O4J contains 0 α-helices and 2 β-strands across 2 chains. 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.

Chains A and B: 0 helices, 1 β-strand

ElementResiduesLengthSheet
β-strand17-2041

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Amyloid-beta precursor proteinA, Bprotein13Homo sapiensP05067 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6O4J_1 Amyloid-beta precursor protein (chains A, B)
XKLVFFAENVGSX

Primary citation

Structure based inhibitors of Amyloid Beta core suggest a common interface with Tau. Griner, S.L., Seidler, P., Bowler, J. et al. Elife (2019) 8. DOI 10.7554/eLife.46924 · PubMed

Other PDB entries of the same protein (UniProt P05067 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

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