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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 DOI10.2210/pdb129l/pdb
DescriptorT4 LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
Functional Keywordshydrolase(o-glycosyl)
Biological sourceEnterobacteria phage T4
Cellular locationHost cytoplasm : P00720
Total number of polymer chains1
Total formula weight18885.56
Authors
Pjura, P.,Matthews, B.W. (deposition date: 1993-05-28, release date: 1994-01-31, Last modification date: 2024-02-07)
Primary citationPjura, 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

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