› 1a4q

X-ray diffraction
1.9Å 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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151094 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuraminidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 390 amino acids
Theoretical weight: 43.43 KDa
Source organism: Influenza B virus (STRAIN B/BEIJING/1/87)
UniProt:
  • Canonical: P27907 (Residues: 76-465; Coverage: 84%)
Gene name: NA
Sequence domains: Neuraminidase
Structure domains: Neuraminidase

Ligands and Environments

3 bound ligands:
Ligand NAG 2 x NAG
Ligand CA 3 x CA
Ligand DPC 2 x DPC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX9.6
Spacegroup: P3121
Unit cell:
a: 88.3Å b: 88.3Å c: 221.1Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.201 0.201 not available

Quick links

Citations

15 review citations

A medicinal chemist's guide to molecular interactions.
Bissantz et al. (2010)
14 more

10 mentions without citation

Consistent improvement of cross-docking results using binding site ensembles generated with elastic network normal modes.
Rueda et al. (2009)
9 more