1L23
ENHANCED PROTEIN THERMOSTABILITY FROM SITE-DIRECTED MUTATIONS THAT DECREASE THE ENTROPY OF UNFOLDING
Summary for 1L23
Entry DOI | 10.2210/pdb1l23/pdb |
Related | 1L01 1L02 1L03 1L04 1L05 1L06 1L07 1L08 1L09 1L10 1L11 1L12 1L13 1L14 1L15 1L16 1L17 1L18 1L19 1L20 1L21 1L22 1L24 1L25 1L26 1L27 1L28 1L29 1L30 1L31 1L32 1L33 1L34 1L35 1L36 2LZM |
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 | 18676.49 |
Authors | Nicholson, H.,Matthews, B.W. (deposition date: 1989-05-01, release date: 1990-01-15, Last modification date: 2024-05-22) |
Primary citation | Matthews, B.W.,Nicholson, H.,Becktel, W.J. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc.Natl.Acad.Sci.USA, 84:6663-6667, 1987 Cited by PubMed: 3477797DOI: 10.1073/pnas.84.19.6663 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
Download full validation report