1hz3 Summary

pdbe.org/1hz3
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ALZHEIMER'S DISEASE AMYLOID-BETA PEPTIDE (RESIDUES 10-35)

The structure was published by Zhang, S., Iwata, K., Lachenmann, M.J., et al., Felix, A.M., Maggio, J.E., and Lee, J.P., in 2000 in a paper entitled "The Alzheimer's peptide a beta adopts a collapsed coil structure in water." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2001.

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

The PDB entry contains the structure of A-BETA AMYLOID. This molecule has the UniProt identifier P05067 (A4_HUMAN)search. The sample contained 26 residues which is < 90% of the natural sequence. Out of 26 residues 26 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 A-BETA AMYLOID P05067 (681-706) (A4_HUMAN)search Homo sapienssearch < 90% 26 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05067 (681 - 706) A-BETA AMYLOID

Chain Structural classification (SCOP) Sequence family (Pfam)
A Amyloid peptidessearch Beta-amyloid peptide (beta-APP)search
Chain InterPro annotation
A Amyloidogenic glycoprotein, amyloid-beta peptidesearch