2BEG: Alzheimer's Abeta(1-42) fibrils

3D Structure of Alzheimer's Abeta(1-42) fibrils. Determined by solution NMR. Released 22 Nov 2005.

Method
Solution NMR
Organism
Homo sapiens
Chains
5
Atoms
900
Mol. weight
22.6 kDa
Released
22 Nov 2005

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

Secondary structure: helices and β-sheets

2BEG contains 0 α-helices and 10 β-strands across 5 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, B, C, D and E: 0 helices, 2 β-strands

ElementResiduesLengthSheet
β-strand18-2691
β-strand31-41112

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Amyloid beta A4 proteinA, B, C, D, Eprotein42Homo sapiensP05067 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E), FASTA
>2BEG_1 Amyloid beta A4 protein (chains A, B, C, D, E)
DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVVIA

Primary citation

3D structure of Alzheimer's amyloid-{beta}(1-42) fibrils. Luhrs, T., Ritter, C., Adrian, M. et al. Proc Natl Acad Sci U S A (2005) 102:17342-17347. DOI 10.1073/pnas.0506723102 · 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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