2MEA

CHANGES IN CONFORMATIONAL STABILITY OF A SERIES OF MUTANT HUMAN LYSOZYMES AT CONSTANT POSITIONS

Summary for 2MEA

DescriptorLYSOZYME (2 entities in total)
Functional Keywordsenzyme, hydrolase, o-glycosyl, alpha + beta, glycosidase
Biological sourceHomo sapiens (human)
Cellular locationSecreted P61626
Total number of polymer chains2
Total molecular weight29509.42
Authors
Funahashi, J.,Takano, K.,Yamagata, Y.,Yutani, K. (deposition date: 1998-05-02, release date: 1998-07-15, Last modification date: 2011-07-13)
Primary citation
Funahashi, J.,Takano, K.,Yamagata, Y.,Yutani, K.
Contribution of amino acid substitutions at two different interior positions to the conformational stability of human lysozyme
Protein Eng., 12:841-850, 1999
PubMed: 10556244 (PDB entries with the same primary citation)
DOI: 10.1093/protein/12.10.841
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.2 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliers904.3%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution