1LWG
Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability
Summary for 1LWG
Entry DOI | 10.2210/pdb1lwg/pdb |
Related | 1LW9 1LWK |
Descriptor | Lysozyme, PHOSPHATE ION, CHLORIDE ION, ... (6 entities in total) |
Functional Keywords | hydrolase (o-glycosyl), t4 lysozyme, methionine core mutant, protein engineering, protein folding, hydrolase |
Biological source | Enterobacteria phage T4 |
Total number of polymer chains | 1 |
Total formula weight | 19503.90 |
Authors | Gassner, N.C.,Baase, W.A.,Mooers, B.H.M.,Busam, R.D.,Weaver, L.H.,Lindstrom, J.D.,Quillin, M.L.,Matthews, B.M. (deposition date: 2002-05-31, release date: 2003-05-20, Last modification date: 2024-02-14) |
Primary citation | Gassner, N.C.,Baase, W.A.,Mooers, B.H.,Busam, R.D.,Weaver, L.H.,Lindstrom, J.D.,Quillin, M.L.,Matthews, B.W. Multiple methionine substitutions are tolerated in T4 lysozyme and have coupled effects on folding and stability. Biophys.Chem., 100:325-340, 2003 Cited by PubMed: 12646375DOI: 10.1016/S0301-4622(02)00290-9 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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