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:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Glycoprotein G and Ephrin-B2 (preferred)
PDBe Complex ID:
PDB-CPX-522680 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glycoprotein G
Molecule details ›
Chains: A, C
Length: 416 amino acids
Theoretical weight: 46.78 KDa
Source organism: Henipavirus hendraense
Expression system: Homo sapiens
UniProt:
Sequence domains: Haemagglutinin-neuraminidase
Structure domains: Neuraminidase
Length: 416 amino acids
Theoretical weight: 46.78 KDa
Source organism: Henipavirus hendraense
Expression system: Homo sapiens
UniProt:
- Canonical:
O89343 (Residues: 188-603; Coverage: 69%)
Sequence domains: Haemagglutinin-neuraminidase
Structure domains: Neuraminidase
Ephrin-B2
Molecule details ›
Chains: B, D
Length: 138 amino acids
Theoretical weight: 15.77 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
Sequence domains: Ephrin
Structure domains: Cupredoxins - blue copper proteins
Length: 138 amino acids
Theoretical weight: 15.77 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
- Canonical: P52799 (Residues: 28-165; Coverage: 45%)
Sequence domains: Ephrin
Structure domains: Cupredoxins - blue copper proteins
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID23-1
Spacegroup:
P212121
Expression system: Homo sapiens
