1OUD
CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V121A MUTANT
Summary for 1OUD
Entry DOI | 10.2210/pdb1oud/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 | 14715.63 |
Authors | Takano, K.,Yamagata, Y.,Fujii, S.,Yutani, K. (deposition date: 1996-08-23, release date: 1997-02-12, Last modification date: 2024-10-16) |
Primary citation | Takano, K.,Yamagata, Y.,Fujii, S.,Yutani, K. Contribution of the hydrophobic effect to the stability of human lysozyme: calorimetric studies and X-ray structural analyses of the nine valine to alanine mutants. Biochemistry, 36:688-698, 1997 Cited by PubMed: 9020766DOI: 10.1021/bi9621829 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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