1WQR

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME

Summary for 1WQR

DescriptorLYSOZYME, SODIUM ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordshydrolase (o-glycosyl), glycosidase, bacteriolytic enzyme, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationSecreted P61626
Total number of polymer chains1
Total molecular weight14798.59
Authors
Yamagata, Y.,Kubota, M.,Sumikawa, Y.,Funahashi, J.,Fujii, S.,Yutani, K. (deposition date: 1998-02-09, release date: 1998-07-01, Last modification date: 2011-07-13)
Primary citation
Yamagata, Y.,Kubota, M.,Sumikawa, Y.,Funahashi, J.,Takano, K.,Fujii, S.,Yutani, K.
Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants.
Biochemistry, 37:9355-9362, 1998
PubMed: 9649316 (PDB entries with the same primary citation)
DOI: 10.1021/bi980431i
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
NMR Information
?

Structure validation

ClashscoreRamachandran outliersSidechain outliers201.9%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution