Multiple Methionine Substitutions are Tolerated in T4 Lysozyme and have Coupled Effects on Folding and Stability

Summary for 1LWK

Related1LW9 1LWG
DescriptorLysozyme, CHLORIDE ION, 2-HYDROXYETHYL DISULFIDE, ... (4 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 weight19766.58
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: 2019-07-24)
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 outliers520 14.0% 6.1%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
Download full validation reportDownload
PDB entries from 2020-09-16