166L

CONTROL OF ENZYME ACTIVITY BY AN ENGINEERED DISULFIDE BOND

Summary for 166L

DescriptorT4 LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL, ... (4 entities in total)
Functional Keywordshydrolase(o-glycosyl)
Biological sourceEnterobacteria phage T4
Cellular locationHost cytoplasm  P00720
Total number of polymer chains1
Total molecular weight18825.51
Authors
Blaber, M.,Matthews, B.W. (deposition date: 1994-06-20, release date: 1994-08-31, Last modification date: 2017-11-29)
Primary citation
Blaber, M.,Baase, W.A.,Gassner, N.,Matthews, B.W.
Alanine scanning mutagenesis of the alpha-helix 115-123 of phage T4 lysozyme: effects on structure, stability and the binding of solvent.
J.Mol.Biol., 246:317-330, 1995
PubMed: 7869383 (PDB entries with the same primary citation)
DOI: 10.1006/jmbi.1994.0087
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.75 Å)
NMR Information
?

Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers503.0%0MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution