› 4mza

X-ray diffraction
1.65Å resolution

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 analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140148 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (5 distinct):
Hemagglutinin-neuraminidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 437 amino acids
Theoretical weight: 48.81 KDa
Source organism: Human parainfluenza 3 virus (strain NIH 47885)
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P08492 (Residues: 136-572; Coverage: 76%)
Gene name: HN
Sequence domains: Haemagglutinin-neuraminidase
Structure domains: Neuraminidase

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, FUL
Carbohydrate polymer
5 bound ligands:
Ligand NAG 2 x NAG
Ligand CA 2 x CA
Ligand EDO 5 x EDO
Ligand SO4 2 x SO4
Ligand PO4 2 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL12-2
Spacegroup: P212121
Unit cell:
a: 83.782Å b: 94.839Å c: 105.499Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.168 0.166 0.198
Expression system: Trichoplusia ni

Quick links

Citations

5 review citations

Measles Virus Fusion Protein: Structure, Function and Inhibition.
Plattet et al. (2016)
4 more

9 mentions without citation

Receptor-mediated cell entry of paramyxoviruses: Mechanisms, and consequences for tropism and pathogenesis.
Navaratnarajah et al. (2020)
8 more