1OUJ

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V99A MUTANT

Summary for 1OUJ

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 weight14715.63
Authors
Takano, K.,Yamagata, Y.,Fujii, S.,Yutani, K. (deposition date: 1996-08-23, release date: 1997-02-12, Last modification date: 2017-11-29)
Primary citation
Takano, K.,Yamagata, Y.,Fujii, S.,Yutani, K.
Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants.
Biochemistry, 36:688-698, 1997
PubMed: 9020766 (PDB entries with the same primary citation)
DOI: 10.1021/bi9621829
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers303.8%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution

More Asymmetric unit images

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