2xzj

X-ray diffraction
1.84Å resolution

THE ASPERGILLUS FUMIGATUS SIALIDASE IS A KDNASE: STRUCTURAL AND MECHANISTIC INSIGHTS

Released:

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.

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175839 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Exo-alpha-sialidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 386 amino acids
Theoretical weight: 42.12 KDa
Source organism: Aspergillus fumigatus Af293
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q4WQS0 (Residues: 21-406; Coverage: 100%)
Gene name: AFUA_4G13800
Sequence domains: BNR repeat-like domain
Structure domains: Neuraminidase

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P21
Unit cell:
a: 75.8Å b: 58.07Å c: 94.4Å
α: 90° β: 99.92° γ: 90°
R-values:
R R work R free
0.204 0.201 0.262
Expression system: Escherichia coli BL21