CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.220 | Intramolecular trans-sialidase; domain 3 |
|
2.40.220.10 | Intramolecular Trans-sialidase; Domain 3 |
Domain Context
CATH Clusters
| Superfamily | Intramolecular Trans-sialidase; Domain 3 |
| Functional Family |
Enzyme Information
| 3.2.1.18 |
Exo-alpha-sialidase.
based on mapping to UniProt Q54727
Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
-!- The enzyme does not act on 4-O-acetylated sialic acids. -!- An endo-alpha-sialidase activity is listed as EC 3.2.1.129. -!- See also EC 4.2.2.15.
|
UniProtKB Entries (1)
| Q54727 |
NANB_STRPN
Streptococcus pneumoniae TIGR4
Sialidase B
|
PDB Structure
| PDB | 4XYX |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Hunt for Serendipitous Allosteric Sites: Discovery of a novel allosteric inhibitor of the bacterial sialidase NanB
To Be Published
|
