CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.5 | Single alpha-helices involved in coiled-coils or other helix-helix interfaces |
|
1.20.5.1240 | Endo-n-acetylneuraminidase |
Domain Context
CATH Clusters
| Superfamily | Endo-n-acetylneuraminidase |
| Functional Family | Tail spike protein |
Enzyme Information
| 3.2.1.129 |
Endo-alpha-sialidase.
based on mapping to UniProt Q04830
Endohydrolysis of (2->8)-alpha-sialosyl linkages in oligo- or poly(sialic) acids.
-!- Although the name endo-N-acetylneuraminidase has also been used for this enzyme, this is misleading since its activity is not restricted to acetyl-substituted substrates. -!- An exo-alpha-sialidase activity is listed as EC 3.2.1.18. -!- See also 4.2.2.15.
|
UniProtKB Entries (1)
| Q04830 |
FIBER_BPK1F
Enterobacteria phage K1F
Tail spike protein
|
PDB Structure
| PDB | 3GW6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of an intramolecular chaperone mediating triple-beta-helix folding.
Nat.Struct.Mol.Biol.
|
