1LYY

AMYLOIDOGENIC VARIANT (ASP67HIS) OF HUMAN LYSOZYME

Summary for 1LYY

DescriptorLYSOZYME (2 entities in total)
Functional Keywordshydrolase, enzyme, beta-1, 4-glycan-hydrolase
Biological sourceHomo sapiens (human)
Cellular locationSecreted P61626
Total number of polymer chains1
Total molecular weight14743.75
Authors
Sunde, M.,Blake, C.C.F. (deposition date: 1997-01-16, release date: 1997-04-01, Last modification date: 2011-07-13)
Primary citation
Booth, D.R.,Sunde, M.,Bellotti, V.,Robinson, C.V.,Hutchinson, W.L.,Fraser, P.E.,Hawkins, P.N.,Dobson, C.M.,Radford, S.E.,Blake, C.C.,Pepys, M.B.
Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis.
Nature, 385:787-793, 1997
PubMed: 9039909 (PDB entries with the same primary citation)
DOI: 10.1038/385787a0
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers2305.7%6.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

Molmil generated image of 1lyy
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Molmil generated image of 1lyy
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Molmil generated image of 1lyy
rotated about y axis by 90°