PDBe 3h72

X-ray diffraction
1.7Å resolution

Crystal structure of Streptococcus pneumoniae D39 neuraminidase A precursor (NanA) in complex with NANA

Released:
Source organism: Streptococcus pneumoniae R6
Primary publication:
Crystal structures of respiratory pathogen neuraminidases.
Biochem. Biophys. Res. Commun. 380 467-71 (2009)
PMID: 19284989

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:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 477 amino acids
Theoretical weight: 53.57 KDa
Source organism: Streptococcus pneumoniae R6
Expression system: Escherichia coli
UniProt:
  • Canonical: P62576 (Residues: 317-793; Coverage: 49%)
Gene names: nanA, spr1536
Sequence domains: BNR/Asp-box repeat
Structure domains: Neuraminidase

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: C2
Unit cell:
a: 158.63Å b: 47.37Å c: 137.06Å
α: 90° β: 116.41° γ: 90°
R-values:
R R work R free
0.175 0.175 0.209
Expression system: Escherichia coli