PDBe 3cye

X-ray diffraction
1.65Å resolution

Cyrstal structure of the native 1918 H1N1 neuraminidase from a crystal with lattice-translocation defects

Released:
Source organism: Influenza A virus
Primary publication:
Structure determination of the 1918 H1N1 neuraminidase from a crystal with lattice-translocation defects.
OpenAccess logo Acta Crystallogr. D Biol. Crystallogr. D64 843-50 (2008)
PMID: 18645233

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 tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuraminidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 387 amino acids
Theoretical weight: 42.49 KDa
Source organism: Influenza A virus
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q9IGQ6 (Residues: 83-469; Coverage: 83%)
Gene name: NA
Sequence domains: Neuraminidase
Structure domains: Neuraminidase

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2221
Unit cell:
a: 117.728Å b: 138.472Å c: 117.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 0.231
Expression system: Trichoplusia ni