1LPY
Multiple Methionine Substitutions in T4 Lysozyme
Summary for 1LPY
Entry DOI | 10.2210/pdb1lpy/pdb |
Related | 1KW5 1KW7 1KY0 1KY1 1L0J 1L0K |
Descriptor | LYSOZYME, PHOSPHATE ION, CHLORIDE ION, ... (5 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 | 19862.95 |
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.W. (deposition date: 2002-05-08, release date: 2002-05-22, Last modification date: 2024-04-03) |
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 (1.65 Å) |
Structure validation
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