› 3cye

X-ray diffraction
1.65Å resolution

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

Released:
DOI: 10.2210/pdb3cye/pdb
PDB entry 3cye coloured by chain, ensemble of 2 models, front view.
PDB entry 3cye coloured by chain, ensemble of 2 models, side view.
PDB entry 3cye coloured by chain, ensemble of 2 models, top view.
Source organism: Influenza A virus
Primary publication:
Structure determination of the 1918 H1N1 neuraminidase from a crystal with lattice-translocation defects.
Zhu X, Xu X, Wilson IA
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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-191526 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
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

Carbohydrate polymer : NEW Components: NAG, MAN
Carbohydrate polymer
5 bound ligands:
Ligand NAG 1 x NAG
Ligand CA 5 x CA
Ligand ACT 5 x ACT
Ligand PO4 1 x PO4
Ligand GOL 10 x GOL
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

Quick links

Citations

1 review citation

Influenza Viruses: Harnessing the Crucial Role of the M2 Ion-Channel and Neuraminidase toward Inhibitor Design.
Mtambo et al. (2021)
13 other articles

5 mentions without citation

phenix.model_vs_data: a high-level tool for the calculation of crystallographic model and data statistics.
Afonine et al. (2010)
4 more