4fnu

X-ray diffraction
3.6Å resolution

Crystal structure of GH36 alpha-galactosidase AgaA A355E D478A from Geobacillus stearothermophilus in complex with stachyose

Released:

Function and Biology Details

Reaction catalysed:
Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Alpha-galactosidase AgaA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 729 amino acids
Theoretical weight: 83.32 KDa
Source organism: Geobacillus stearothermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9ALJ4 (Residues: 1-729; Coverage: 100%)
Gene name: agaA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLA, GLC, FRU
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: P3221
Unit cell:
a: 154.07Å b: 154.07Å c: 238.02Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.24 0.238 0.282
Expression system: Escherichia coli