2beg Summary

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3D Structure of Alzheimer's Abeta(1-42) fibrils

The structure was published by Luhrs, T., Ritter, C., Adrian, M., et al., Dobeli, H., Schubert, D., and Riek, R., in 2005 in a paper entitled "3D structure of Alzheimer's amyloid-{beta}(1-42) fibrils." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2005.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of Amyloid beta A4 protein.

The molecule most likely forms homopentamers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Amyloid beta A4 protein P05067 (672-713) (A4_HUMAN)search Homo sapienssearch < 90% 42 61%
B Amyloid beta A4 protein P05067 (672-713) (A4_HUMAN)search Homo sapienssearch < 90% 42 61%
C Amyloid beta A4 protein P05067 (672-713) (A4_HUMAN)search Homo sapienssearch < 90% 42 61%
D Amyloid beta A4 protein P05067 (672-713) (A4_HUMAN)search Homo sapienssearch < 90% 42 61%
E Amyloid beta A4 protein P05067 (672-713) (A4_HUMAN)search Homo sapienssearch < 90% 42 61%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05067 (672 - 713) Amyloid beta A4 protein Homo sapiens

Chain Sequence family (Pfam)
A, B, C, D, E Beta-amyloid peptide (beta-APP)search

Chain ID Biological process (GO) Cellular component (GO)
A, B, C, D, E (P05067) nervous system developmentsearch integral component of membranesearch

Chain InterPro annotation
A, B, C, D, E Amyloidogenic glycoprotein, amyloid-beta peptidesearch Amyloid beta A4 proteinsearch