1L45
CUMULATIVE SITE-DIRECTED CHARGE-CHANGE REPLACEMENTS IN BACTERIOPHAGE T4 LYSOZYME SUGGEST THAT LONG-RANGE ELECTROSTATIC INTERACTIONS CONTRIBUTE LITTLE TO PROTEIN STABILITY
Summary for 1L45
Entry DOI | 10.2210/pdb1l45/pdb |
Descriptor | T4 LYSOZYME (2 entities in total) |
Functional Keywords | hydrolase (o-glycosyl) |
Biological source | Enterobacteria phage T4 |
Cellular location | Host cytoplasm : P00720 |
Total number of polymer chains | 1 |
Total formula weight | 18662.40 |
Authors | Daopin, S.,Matthews, B.W. (deposition date: 1991-01-28, release date: 1991-10-15, Last modification date: 2024-05-22) |
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 Cited by PubMed: 1942034DOI: 10.1016/0022-2836(91)80181-S PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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