1YAQ
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 1YAQ
Entry DOI | 10.2210/pdb1yaq/pdb |
Descriptor | LYSOZYME, SODIUM ION (3 entities in total) |
Functional Keywords | hydrolase |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P61626 |
Total number of polymer chains | 1 |
Total formula weight | 14729.66 |
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 citation | Takano, 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: 7473760DOI: 10.1006/jmbi.1995.0599 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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