Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1OUC

CONTRIBUTION OF HYDROPHOBIC RESIDUES TO THE STABILITY OF HUMAN LYSOZYME: X-RAY STRUCTURE OF THE V110A MUTANT

Summary for 1OUC
Entry DOI10.2210/pdb1ouc/pdb
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: 2021-11-03)
Primary citationTakano, 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: 9020766
DOI: 10.1021/bi9621829
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.8 Å)
Structure validation

217157

건을2024-03-13부터공개중

PDB statisticsPDBj update infoContact PDBjnumon