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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
Entry DOI10.2210/pdb1b5y/pdb
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 formula 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: 2021-11-03)
Primary citationTakano, 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
Cited by
PubMed: 10350481
DOI: 10.1021/bi9901228
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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