131L

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 131L

Entry DOI	10.2210/pdb131l/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	18841.51
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: 8298466 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation