4sli is a 1 chain structure with sequence from Macde. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Intramolecular trans-sialidase from leech (Macrobdella decora) is the first member of the sialidase superfamily found to exhibit strict specificity towards the cleavage of terminal Neu5Acalpha2-->3Gal linkage in sialoglycoconjugates. Its release of 2,7-anhydro-Neu5Ac instead of Neu5Ac indicates that it catalyzes an intramolecular trans-sialosyl reaction. Crystal structures of its complexes with an inactive substrate analogue 2-propenyl-Neu5Ac, and with the product 2,7-anhydro-Neu5Ac, have been determined to 1.8 A resolution. The boat conformation of the pyranose observed in the complexes supports the proposed enzymatic mechanism that O7 of an axial 6-glycerol group attacks the positively charged C2 of the intermediate. A generalized mechanism is proposed for the sialidase superfamily.
The 1.8 A structures of leech intramolecular trans-sialidase complexes: evidence of its enzymatic mechanism.,Luo Y, Li SC, Li YT, Luo M J Mol Biol. 1999 Jan 8;285(1):323-32. PMID:9878409[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Luo Y, Li SC, Li YT, Luo M. The 1.8 A structures of leech intramolecular trans-sialidase complexes: evidence of its enzymatic mechanism. J Mol Biol. 1999 Jan 8;285(1):323-32. PMID:9878409 doi:10.1006/jmbi.1998.2345
