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: 9010773 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.8 Å)

Structure validation