1amc Summary

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SOLUTION STRUCTURE OF RESIDUES 1-28 OF THE AMYLOID BETA-PEPTIDE

The structure was published by Talafous, J., Marcinowski, K.J., Klopman, G., and Zagorski, M.G., in 1994 in a paper entitled "Solution structure of residues 1-28 of the amyloid beta-peptide." (abstract).

The structure was determined using NMR spectroscopy and deposited in 1994.

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

The PDB entry contains the structure of AMYLOID BETA-PEPTIDE. This molecule has the UniProt identifier P05067 (A4_HUMAN)search. The sample contained 28 residues which is < 90% of the natural sequence. Out of 28 residues 28 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 BETA-PEPTIDE P05067 (672-699) (A4_HUMAN)search Homo sapienssearch < 90% 28 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05067 (672 - 699) AMYLOID BETA-PEPTIDE Homo sapiens

Chain Structural classification (SCOP) Sequence family (Pfam)
A Amyloid peptidessearch 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