1DYB
DETERMINATION OF ALPHA-HELIX PROPENSITY WITHIN THE CONTEXT OF A FOLDED PROTEIN: SITES 44 AND 131 IN BACTERIOPHAGE T4 LYSOZYME
Summary for 1DYB
Entry DOI | 10.2210/pdb1dyb/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 | 18847.56 |
Authors | Zhang, X.,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: 8289284DOI: 10.1006/jmbi.1994.1016 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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