1CQN

PROTEIN AGGREGATION AND ALZHEIMER'S DISEASE: CRYSTALLOGRAPHIC ANALYSIS OF THE PHENOMENON. ENGINEERED VERSION OF THE RIBOSOMAL PROTEIN S6 USED AS A STABLE SCAFFOLD TO STUDY OLIGOMERIZATION.

Summary for 1CQN

Related1CQM 1QJH
DescriptorRIBOSOMAL PROTEIN S6 (2 entities in total)
Functional Keywordsalzheimer disease, ribosomal protein s6, oligomerization, ribosomal protein
Biological sourceThermus thermophilus
Total number of polymer chains2
Total molecular weight23829.52
Authors
Kristensen, O.,Otzen, D.E.,Oliveberg, M. (deposition date: 1999-08-08, release date: 2000-09-08, Last modification date: 2018-03-14)
Primary citation
Otzen, D.E.,Kristensen, O.,Oliveberg, M.
Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly.
Proc.Natl.Acad.Sci.USA, 97:9907-9912, 2000
PubMed: 10944185 (PDB entries with the same primary citation)
DOI: 10.1073/pnas.160086297
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.1 Å)
NMR Information
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Structure validation

RfreeClashscoreRamachandran outliersSidechain outliersRSRZ outliers0.276901.1%2.6%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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More Biological unit images

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(*)In the case of coarse surface representation, the asymmetric unit is shown as red ribbon representation.
Coordinate files for Biological unit (1cqn.pdb1.gz [19.36 KB])
Coordinate files for Biological unit (1cqn.pdb2.gz [19.66 KB])