Near-atomic resolution fibril structure of complete amyloid-beta(1-42) by cryo-EM. Determined by electron microscopy at 4.0 Å resolution. Released 13 Sept 2017.
Explore 5OQV in 3D Show helices and sheets RCSB PDB PDBe
5OQV contains 0 α-helices and 27 β-strands across 9 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-22 | 20 | 1 |
| β-strand | 28-35 | 8 | 2 |
| β-strand | 40-41 | 2 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Amyloid beta A4 protein | A, B, C, D, E, F, G, H, I | protein | 42 | Homo sapiens | P05067 (AlphaFold model) |
>5OQV_1 Amyloid beta A4 protein (chains A, B, C, D, E, F, G, H, I) DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA
Fibril structure of amyloid-beta (1-42) by cryo-electron microscopy. Gremer, L., Scholzel, D., Schenk, C. et al. Science (2017) 358:116-119. DOI 10.1126/science.aao2825 · PubMed
Other PDB entries of the same protein (UniProt P05067 (AlphaFold model), which also has an AlphaFold model), best resolution first:
5OQV is part of these collections:
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