129L
STRUCTURES OF RANDOMLY GENERATED MUTANTS OF T4 LYSOZYME SHOW THAT PROTEIN STABILITY CAN BE ENHANCED BY RELAXATION OF STRAIN AND BY IMPROVED HYDROGEN BONDING VIA BOUND SOLVENT
Summary for 129L
Entry DOI | 10.2210/pdb129l/pdb |
Descriptor | T4 LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total) |
Functional Keywords | hydrolase(o-glycosyl) |
Biological source | Enterobacteria phage T4 |
Cellular location | Host cytoplasm : P00720 |
Total number of polymer chains | 1 |
Total formula weight | 18885.56 |
Authors | Pjura, P.,Matthews, B.W. (deposition date: 1993-05-28, release date: 1994-01-31, Last modification date: 2024-02-07) |
Primary citation | Pjura, P.,Matthews, B.W. Structures of randomly generated mutants of T4 lysozyme show that protein stability can be enhanced by relaxation of strain and by improved hydrogen bonding via bound solvent. Protein Sci., 2:2226-2232, 1993 Cited by PubMed: 8298466PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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