1DYG

DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME

Summary for 1DYG

Entry DOI	10.2210/pdb1dyg/pdb
Descriptor	T4 LYSOZYME, CHLORIDE ION, BETA-MERCAPTOETHANOL, ... (4 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	18919.62
Authors	Zhou, H.-J.,Matthews, B.W. (deposition date: 1993-05-13, release date: 1993-10-31, Last modification date: 2017-11-29)
Primary citation	Blaber, M.,Zhang, X.J.,Lindstrom, J.D.,Pepiot, S.D.,Baase, W.A.,Matthews, B.W. Determination of alpha-helix propensity within the context of a folded protein. Sites 44 and 131 in bacteriophage T4 lysozyme. J.Mol.Biol., 235:600-624, 1994 Cited by PubMed: 8289284 DOI: 10.1006/jmbi.1994.1016 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation