4mze

X-ray diffraction
1.8Å resolution

Crystal structure of hPIV3 hemagglutinin-neuraminidase, H552Q/Q559R mutant

Released:

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:
homo dimer (preferred)
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: 48.82 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 : NEW Components: NAG, FUL
Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer : NEW Components: NAG, BMA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P212121
Unit cell:
a: 84.029Å b: 96.643Å c: 105.339Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.161 0.196
Expression system: Trichoplusia ni