1WQQ
CONTRIBUTION OF HYDROGEN BONDS TO THE CONFORMATIONAL STABILITY OF HUMAN LYSOZYME
Summary for 1WQQ
Entry DOI | 10.2210/pdb1wqq/pdb |
Descriptor | LYSOZYME, SODIUM ION, CHLORIDE ION, ... (4 entities in total) |
Functional Keywords | hydrolase (o-glycosyl), glycosidase, bacteriolytic enzyme, hydrolase |
Biological source | Homo sapiens (human) |
Cellular location | Secreted: P61626 |
Total number of polymer chains | 1 |
Total formula weight | 14798.59 |
Authors | Yamagata, Y.,Kubota, M.,Sumikawa, Y.,Funahashi, J.,Fujii, S.,Yutani, K. (deposition date: 1998-02-09, release date: 1998-07-01, Last modification date: 2024-04-03) |
Primary citation | Yamagata, Y.,Kubota, M.,Sumikawa, Y.,Funahashi, J.,Takano, K.,Fujii, S.,Yutani, K. Contribution of hydrogen bonds to the conformational stability of human lysozyme: calorimetry and X-ray analysis of six tyrosine --> phenylalanine mutants. Biochemistry, 37:9355-9362, 1998 Cited by PubMed: 9649316DOI: 10.1021/bi980431i PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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