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1LPY

Multiple Methionine Substitutions in T4 Lysozyme

Summary for 1LPY
Entry DOI10.2210/pdb1lpy/pdb
Related1KW5 1KW7 1KY0 1KY1 1L0J 1L0K
DescriptorLYSOZYME, PHOSPHATE ION, CHLORIDE ION, ... (5 entities in total)
Functional Keywordshydrolase (o-glycosyl), t4 lysozyme, methionine core mutant, protein engineering, protein folding, hydrolase
Biological sourceEnterobacteria phage T4
Total number of polymer chains1
Total formula weight19862.95
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: 2021-10-27)
Primary citationGassner, 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: 12646375
DOI: 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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