X-ray diffraction
2Å resolution

Crystal structure of Streptococcus pneumoniae NanA (TIGR4) in complex with DANA


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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Sialidase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 493 amino acids
Theoretical weight: 55.35 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli BL21
  • Canonical: P62575 (Residues: 318-792; Coverage: 48%)
Gene name: nanA
Sequence domains: BNR repeat-like domain
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: C2
Unit cell:
a: 164.857Å b: 48.835Å c: 125.383Å
α: 90° β: 104.13° γ: 90°
R R work R free
0.197 0.196 0.238
Expression system: Escherichia coli BL21