1B5Y

CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME: CALORIMETRY AND X-RAY ANALYSIS OF SIX SER->ALA MUTANTS

Summary for 1B5Y

DescriptorPROTEIN (LYSOZYME), SODIUM ION (3 entities in total)
Functional Keywordshydrogen bond, stability, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationSecreted P61626
Total number of polymer chains1
Total molecular weight14727.68
Authors
Takano, K.,Yamagata, Y.,Kubota, M.,Funahashi, J.,Fujii, S.,Yutani, K. (deposition date: 1999-01-11, release date: 1999-01-20, Last modification date: 2011-07-13)
Primary citation
Takano, K.,Yamagata, Y.,Kubota, M.,Funahashi, J.,Fujii, S.,Yutani, K.
Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six Ser --> Ala mutants.
Biochemistry, 38:6623-6629, 1999
PubMed: 10350481 (PDB entries with the same primary citation)
DOI: 10.1021/bi9901228
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (2.2 Å)
NMR Information
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Structure validation

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