Multiple Methionine Substitutions in T4 Lysozyme

Summary for 1LPY

Related1L0K 1KY1 1L0J 1KW7 1KY0 1KW5
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 molecular weight19862.95
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: 2011-07-13)
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
PubMed: 12646375 (PDB entries with the same primary citation)
DOI: 10.1016/S0301-4622(02)00290-9
MImport into Mendeley
Experimental method

Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers310 11.8% 0.7%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-09-23