› 1nna

X-ray diffraction
2.5Å resolution

THREE-DIMENSIONAL STRUCTURE OF INFLUENZA A N9 NEURAMINIDASE AND ITS COMPLEX WITH THE INHIBITOR 2-DEOXY 2,3-DEHYDRO-N-ACETYL NEURAMINIC ACID

Released:
DOI: 10.2210/pdb1nna/pdb
PDB entry 1nna coloured by chain, front view.
PDB entry 1nna coloured by chain, side view.
PDB entry 1nna coloured by chain, top view.
Source organism: Influenza A virus
Primary publication:
Three-dimensional structure of influenza A N9 neuraminidase and its complex with the inhibitor 2-deoxy 2,3-dehydro-N-acetyl neuraminic acid.
Bossart-Whitaker P, Carson M, Babu YS, Smith CD, Laver WG, Air GM
J Mol Biol 232 1069-83 (1993)
PMID: 8371267

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-137058 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Neuraminidase Chain: A
Molecule details ›
Chain: A
Length: 387 amino acids
Theoretical weight: 43.57 KDa
Source organism: Influenza A virus
Expression system: Not provided
UniProt:
  • Canonical: P03472 (Residues: 84-470; Coverage: 82%)
Gene name: NA
Sequence domains: Neuraminidase
Structure domains: Neuraminidase

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: I432
Unit cell:
a: 183.78Å b: 183.78Å c: 183.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.193 0.193 not available
Expression system: Not provided

Quick links

Citations

20 review citations

Mechanisms of enzymatic glycoside hydrolysis.
McCarter et al. (1994)
19 more

10 mentions without citation

Cellobiose dehydrogenase modified electrodes: advances by materials science and biochemical engineering.
Ludwig et al. (2013)
9 more