1OUJ

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V99A MUTANT

Summary for 1OUJ
DescriptorLYSOZYME, SODIUM ION (3 entities in total)
Functional Keywordshydrolase (o-glycosyl), amyloid, disease mutation
Biological sourceHomo sapiens (human)
Cellular locationSecreted: P61626
Total number of polymer chains1
Total formula weight14715.63
Authors
Takano, K.,Yamagata, Y.,Fujii, S.,Yutani, K. (deposition date: 1996-08-23, release date: 1997-02-12, Last modification date: 2017-11-29)
Primary citationFujii, S.,Takano, K.,Yamagata, Y.,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
PubMed: 9020766
DOI: 110.1021/bi9621829
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation
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PDB entries from 2021-06-16