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X-ray diffraction
1.84Å resolution

Carbohydrate binding domain from Streptococcus pneumoniae NanA sialidase

Released:
Source organism: Streptococcus pneumoniae
Entry authors: Yang L, Connaris H, Potter JA, Taylor GL

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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158647 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Sialidase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 188 amino acids
Theoretical weight: 21.07 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P62575 (Residues: 121-305; Coverage: 19%)
Gene name: nanA
Sequence domains: Sialidase, N-terminal domain
Structure domains: Jelly Rolls

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 39.234Å b: 66.984Å c: 66.792Å
α: 90° β: 92.43° γ: 90°
R-values:
R R work R free
0.165 0.162 0.208
Expression system: Escherichia coli