154L
THE REFINED STRUCTURES OF GOOSE LYSOZYME AND ITS COMPLEX WITH A BOUND TRISACCHARIDE SHOW THAT THE "GOOSE-TYPE LYSOZYMES LACK A CATALYTIC ASPARTATE
Summary for 154L
Entry DOI | 10.2210/pdb154l/pdb |
Related PRD ID | PRD_900017 |
Descriptor | GOOSE LYSOZYME, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
Functional Keywords | hydrolase(o-glycosyl) |
Cellular location | Secreted: P00718 |
Total number of polymer chains | 1 |
Total formula weight | 21033.73 |
Authors | Weaver, L.H.,Gruetter, M.G.,Matthews, B.W. (deposition date: 1994-05-05, release date: 1995-01-26, Last modification date: 2020-07-29) |
Primary citation | Weaver, L.H.,Grutter, M.G.,Matthews, B.W. The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue. J.Mol.Biol., 245:54-68, 1995 Cited by PubMed: 7823320DOI: 10.1016/S0022-2836(95)80038-7 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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