1DXJ
Structure of the chitinase from jack bean
Summary for 1DXJ
Entry DOI | 10.2210/pdb1dxj/pdb |
Related | 1CNS 1CTN 1D2K |
Descriptor | CLASS II CHITINASE, SULFATE ION (3 entities in total) |
Functional Keywords | hydrolase, family 19 glycosidase, alpha helical protein |
Biological source | CANAVALIA ENSIFORMIS (JACK BEAN) |
Total number of polymer chains | 1 |
Total formula weight | 26235.08 |
Authors | Hahn, M.,Hennig, M.,Schlesier, B.,Hohne, W. (deposition date: 2000-01-10, release date: 2000-08-29, Last modification date: 2024-10-16) |
Primary citation | Hahn, M.,Hennig, M.,Schlesier, B.,Hohne, W. Structure of Jack Bean Chitinase Acta Crystallogr.,Sect.D, 56:1096-, 2000 Cited by PubMed Abstract: The structure of jack bean chitinase was solved at 1.8 A resolution by molecular replacement. It is an alpha-helical protein with three disulfide bridges. The active site is related in structure to animal and viral lysozymes. However, unlike in lysozyme, the architecture of the active site suggests a single-step cleavage. According to this mechanism, Glu68 is the proton donor and Glu90 assists in the reaction by moving towards the substrate and recruiting a water molecule that acts as the nucleophile. In this model, a water molecule was found in contact with Glu90 O(epsilon1) and Thr119 O(gamma) at a distance of 3.0 and 2.8 A, respectively. The model is in accordance with the observed inversion mechanism. PubMed: 10957628DOI: 10.1107/S090744490000857X PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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