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1YAO

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 1YAO
Entry DOI10.2210/pdb1yao/pdb
DescriptorLYSOZYME, SODIUM ION (3 entities in total)
Functional Keywordshydrolase
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P61626
Total number of polymer chains1
Total formula 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: 2021-11-03)
Primary citationTakano, 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
Cited by
PubMed: 7473760
DOI: 10.1006/jmbi.1995.0599
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

217705

数据于2024-03-27公开中

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