1L13

CONTRIBUTIONS OF HYDROGEN BONDS OF THR 157 TO THE THERMODYNAMIC STABILITY OF PHAGE T4 LYSOZYME

Summary for 1L13

Entry DOI	10.2210/pdb1l13/pdb
Related	1L01 1L02 1L03 1L04 1L05 1L06 1L07 1L08 1L09 1L10 1L11 1L12 1L14 1L15 1L16 1L17 1L18 1L19 1L20 1L21 1L22 1L23 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	18718.56
Authors	Dao-Pin, S.,Alber, T.,Matthews, B.W. (deposition date: 1988-02-05, release date: 1988-04-16, Last modification date: 2024-05-22)
Primary citation	Alber, T.,Sun, D.P.,Wilson, K.,Wozniak, J.A.,Cook, S.P.,Matthews, B.W. Contributions of hydrogen bonds of Thr 157 to the thermodynamic stability of phage T4 lysozyme. Nature, 330:41-46, 1987 Cited by PubMed Abstract: Measurements of changes in structure and stability caused by 13 different substitutions for threonine 157 in phage T4 lysozyme show that the most stable lysozyme variants contain hydrogen bonds analogous to those in the wild-type enzyme and that structural adjustments allow the protein to be surprisingly tolerant of amino-acid substitutions. PubMed: 3118211 DOI: 10.1038/330041a0 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation