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:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Sialidase A (preferred)
PDBe Complex ID:
PDB-CPX-158649 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase A
Molecule details ›
Chains: A, B
Length: 471 amino acids
Theoretical weight: 52.95 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: BNR/Asp-box repeat
Structure domains:
Length: 471 amino acids
Theoretical weight: 52.95 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P62576 (Residues: 321-791; Coverage: 48%)
Sequence domains: BNR/Asp-box repeat
Structure domains:
