PDBe 2xcy

X-ray diffraction
1.84Å resolution

Crystal structure of Aspergillus fumigatus sialidase


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. 
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Exo-alpha-sialidase Chains: A, B
Molecule details ›
Chains: A, B
Length: 386 amino acids
Theoretical weight: 42.35 KDa
Source organism: Aspergillus fumigatus
Expression system: Escherichia coli BL21
  • Canonical: Q4WQS0 (Residues: 21-406; Coverage: 100%)
Gene name: AFUA_4G13800
Sequence domains: BNR repeat-like domain
Structure domains: Neuraminidase

Ligands and Environments

2 bound ligands:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P21
Unit cell:
a: 75.89Å b: 58.19Å c: 94.7Å
α: 90° β: 100.01° γ: 90°
R R work R free
0.155 0.153 0.194
Expression system: Escherichia coli BL21