1YAP

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: CALORIMETRIC STUDIES AND X-RAY STRUCTURAL ANALYSIS OF THE FIVE ISOLEUCINE TO VALINE MUTANTS

Summary for 1YAP

DescriptorLYSOZYME, SODIUM ION (3 entities in total)
Functional Keywordshydrolase
Biological sourceHomo sapiens (human)
Cellular locationSecreted P61626
Total number of polymer chains1
Total molecular weight14729.66
Authors
Yamagata, Y.,Kaneda, H.,Fujii, S.,Takano, K.,Ogasahara, K.,Kanaya, E.,Kikuchi, M.,Oobatake, M.,Yutani, K. (deposition date: 1995-09-29, release date: 1996-04-03, Last modification date: 2017-11-29)
Primary citation
Takano, K.,Ogasahara, K.,Kaneda, H.,Yamagata, Y.,Fujii, S.,Kanaya, E.,Kikuchi, M.,Oobatake, M.,Yutani, K.
Contribution of hydrophobic residues to the stability of human lysozyme: calorimetric studies and X-ray structural analysis of the five isoleucine to valine mutants.
J.Mol.Biol., 254:62-76, 1995
PubMed: 7473760 (PDB entries with the same primary citation)
DOI: 10.1006/jmbi.1995.0599
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers302.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution