Function and Biology Details
Reaction catalysed:
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.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
exo-alpha-sialidase (preferred)
PDBe Complex ID:
PDB-CPX-493741 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
exo-alpha-sialidase
Molecule details ›
Chain: A
Length: 143 amino acids
Theoretical weight: 15.38 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains: Immunoglobulin-like
Length: 143 amino acids
Theoretical weight: 15.38 KDa
Source organism: Clostridium perfringens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A0A0H2YT71 (Residues: 939-1081; Coverage: 12%)
Structure domains: Immunoglobulin-like
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
RIGAKU MICROMAX-002
Spacegroup:
P4322
Expression system: Escherichia coli BL21(DE3)
