1OUA
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE I56T MUTANT
Summary for 1OUA
Entry DOI | 10.2210/pdb1oua/pdb |
Descriptor | LYSOZYME, SODIUM ION (3 entities in total) |
Functional Keywords | hydrolase (o-glycosyl), amyloid, disease mutation |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P61626 |
Total number of polymer chains | 1 |
Total formula weight | 14731.63 |
Authors | Takano, K.,Funahashi, J.,Yamagata, Y.,Ogasahara, K.,Yutani, K. (deposition date: 1996-08-23, release date: 1997-02-12, Last modification date: 2017-11-29) |
Primary citation | Funahashi, J.,Takano, K.,Ogasahara, K.,Yamagata, Y.,Yutani, K. The structure, stability, and folding process of amyloidogenic mutant human lysozyme. J.Biochem.(Tokyo), 120:1216-1223, 1996 Cited by PubMed: 9010773PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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