1aml Summary

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THE ALZHEIMER`S DISEASE AMYLOID A4 PEPTIDE (RESIDUES 1-40)

The structure was published by Sticht, H., Bayer, P., Willbold, D., et al., Beyreuther, K., Frank, R.W., and Rosch, P., in 1995 in a paper entitled "Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease." (abstract).

The structure was determined using NMR spectroscopy and deposited in 1995.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of AMYLOID A4. This molecule has the UniProt identifier P05067 (A4_HUMAN)search. The sample contained 40 residues which is < 90% of the natural sequence. Out of 40 residues 40 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

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 A4 P05067 (672-711) (A4_HUMAN)search Homo sapienssearch < 90% 40 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05067 (672 - 711) AMYLOID A4 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A Amyloid peptidessearch Amyloid A4search Beta-amyloid peptide (beta-APP)search

Chain ID Cellular component (GO)
A (P05067) integral to membranesearch

Chain InterPro annotation
A Amyloidogenic glycoprotein, amyloid-beta peptidesearch