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:
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Sialidase-2 (preferred)
PDBe Complex ID:
PDB-CPX-195217 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase-2
Molecule details ›
Chain: A
Length: 382 amino acids
Theoretical weight: 42.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: BNR repeat-like domain
Structure domains: Neuraminidase
Length: 382 amino acids
Theoretical weight: 42.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
Q9Y3R4 (Residues: 1-380; Coverage: 100%)
Sequence domains: BNR repeat-like domain
Structure domains: Neuraminidase
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup:
R3
Expression system: Escherichia coli BL21
