1LLO
HEVAMINE A (A PLANT ENDOCHITINASE/LYSOZYME) COMPLEXED WITH ALLOSAMIDIN
Summary for 1LLO
| Entry DOI | 10.2210/pdb1llo/pdb |
| Related PRD ID | PRD_000468 |
| Descriptor | Hevamine-A, 2-acetamido-2-deoxy-beta-D-allopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-allopyranose, ALLOSAMIZOLINE, ... (4 entities in total) |
| Functional Keywords | chitinase, lysozyme, hydrolase |
| Biological source | Hevea brasiliensis (rubber tree) |
| Cellular location | Vacuole: P23472 |
| Total number of polymer chains | 1 |
| Total formula weight | 30213.82 |
| Authors | Terwisscha Van Scheltinga, A.C.,Armand, S.,Kalk, K.H.,Isogai, A.,Henrissat, B.,Dijkstra, B.W. (deposition date: 1995-11-08, release date: 1996-03-08, Last modification date: 2024-10-30) |
| Primary citation | Terwisscha van Scheltinga, A.C.,Armand, S.,Kalk, K.H.,Isogai, A.,Henrissat, B.,Dijkstra, B.W. Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry, 34:15619-15623, 1995 Cited by PubMed Abstract: The plant enzyme hevamine has both chitinase and lysozyme activity. HPLC analysis of the products of the hydrolysis of chitopentaose shows that hevamine acts with retention of the configuration, despite the absence of a nucleophilic or stabilizing carboxylate. To analyze the stabilization of a putative oxocarbonium ion intermediate, the X-ray structure of hevamine complexed with the inhibitor allosamidin was determined at 1.85 A resolution. This structure supports the role of Glu127 as a proton donor. The allosamizoline group binds in the center of the active site, mimicking a reaction intermediate in which a positive charge at C1 is stabilized intramolecularly by the carbonyl oxygen of the N-acetyl group at C2. PubMed: 7495789DOI: 10.1021/bi00048a003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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