1mwp Summary



The structure was published by Rossjohn, J., Cappai, R., Feil, S.C., et al., Beyreuther, K., Masters, C.L., and Parker, M.W., in 1999 in a paper entitled "Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.8 Å and deposited in 1999.

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

The PDB entry contains the structure of AMYLOID A4 PROTEIN. This molecule has the UniProt identifier P05067 (A4_HUMAN)search. The sample contained 96 residues which is < 90% of the natural sequence. Out of 96 residues 96 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 PROTEIN P05067 (28-123) (A4_HUMAN)search Homo sapienssearch < 90% 96 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P05067 (28 - 123) AMYLOID A4 PROTEIN Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A A heparin-binding domainsearch Sugar Binding Protein, Amyloid A4 Protein; Chain Asearch Amyloid A4 N-terminal heparin-bindingsearch

Chain ID Biological process (GO) Molecular function (GO)
A (P05067) nervous system developmentsearch heparin bindingsearch

Chain InterPro annotation
A Amyloidogenic glycoprotein, heparin-bindingsearch Amyloid beta A4 proteinsearch