1HVQ
CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND ITS COMPLEX WITH AN INHIBITOR
Summary for 1HVQ
Entry DOI | 10.2210/pdb1hvq/pdb |
Related PRD ID | PRD_900017 |
Descriptor | HEVAMINE A, 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 | glycosidase, chitin degradation, multifunctional enzyme, hydrolase |
Biological source | Hevea brasiliensis |
Cellular location | Vacuole: P23472 |
Total number of polymer chains | 1 |
Total formula weight | 30200.78 |
Authors | Terwisscha Van Scheltinga, A.C.,Kalk, K.H.,Beintema, J.J.,Dijkstra, B.W. (deposition date: 1994-10-13, release date: 1995-12-02, Last modification date: 2024-10-09) |
Primary citation | Terwisscha van Scheltinga, A.C.,Kalk, K.H.,Beintema, J.J.,Dijkstra, B.W. Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure, 2:1181-1189, 1994 Cited by PubMed Abstract: Hevamine is a member of one of several families of plant chitinases and lysozymes that are important for plant defence against pathogenic bacteria and fungi. The enzyme can hydrolyze the linear polysaccharide chains of chitin and peptidoglycan. A full understanding of the structure/function relationships of chitinases might facilitate the production of transgenic plants with increased resistance towards a wide range of pathogens. PubMed: 7704528DOI: 10.1016/S0969-2126(94)00120-0 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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