1L43

CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY

Summary for 1L43

DescriptorT4 LYSOZYME (2 entities in total)
Functional Keywordshydrolase (o-glycosyl)
Biological sourceEnterobacteria phage T4
Cellular locationHost cytoplasm  P00720
Total number of polymer chains1
Total molecular weight18662.4
Authors
Daopin, S.,Matthews, B.W. (deposition date: 1991-01-28, release date: 1991-10-15, Last modification date: 2017-11-29)
Primary citation
Sun, D.P.,Soderlind, E.,Baase, W.A.,Wozniak, J.A.,Sauer, U.,Matthews, B.W.
Cumulative site-directed charge-change replacements in bacteriophage T4 lysozyme suggest that long-range electrostatic interactions contribute little to protein stability.
J.Mol.Biol., 221:873-887, 1991
PubMed: 1942034 (PDB entries with the same primary citation)
DOI: 10.1016/0022-2836(91)80181-S
MImport into Mendeley
Experimental method
X-RAY DIFFRACTION (1.8 Å)
NMR Information
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Structure validation

ClashscoreRamachandran outliersSidechain outliersRSRZ outliers802.9%3.8%MetricValuePercentile RanksWorseBetterPercentile relative to all X-ray structuresPercentile relative to X-ray structures of similar resolution
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