1OUA

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE I56T MUTANT

Summary for 1OUA

DescriptorLYSOZYME, SODIUM ION (3 entities in total)
Functional Keywordshydrolase (o-glycosyl), amyloid, disease mutation
Biological sourceHomo sapiens (human)
Cellular locationSecreted P61626
Total number of polymer chains1
Total molecular weight14731.63
Authors
Takano, K.,Funahashi, J.,Yamagata, Y.,Ogasahara, K.,Yutani, K. (deposition date: 1996-08-23, release date: 1997-02-12, Last modification date: 2017-11-29)
Primary citation
Funahashi, J.,Takano, K.,Ogasahara, K.,Yamagata, Y.,Yutani, K.
The structure, stability, and folding process of amyloidogenic mutant human lysozyme.
J.Biochem.(Tokyo), 120:1216-1223, 1996
PubMed: 9010773 (PDB entries with the same primary citation)
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers601.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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