› 4fnr

X-ray diffraction
3.2Å resolution

Crystal structure of GH36 alpha-galactosidase AgaA from Geobacillus stearothermophilus

Released:
DOI: 10.2210/pdb4fnr/pdb
PDB entry 4fnr coloured by chain, front view.
PDB entry 4fnr coloured by chain, side view.
PDB entry 4fnr coloured by chain, top view.
Source organism: Geobacillus stearothermophilus
Primary publication:
The molecular mechanism of thermostable α-galactosidases AgaA and AgaB explained by x-ray crystallography and mutational studies.
Merceron R, Foucault M, Haser R, Mattes R, Watzlawick H, Gouet P
J Biol Chem 287 39642-52 (2012)
PMID: 23012371

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
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189575 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-galactosidase AgaA Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 729 amino acids
Theoretical weight: 83.31 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

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P3221
Unit cell:
a: 150Å b: 150Å c: 233Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.177 0.174 0.226
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Biotechnological potential of microbial α-galactosidases.
Katrolia et al. (2014)
5 more

1 mention without citation

The molecular mechanism of thermostable α-galactosidases AgaA and AgaB explained by x-ray crystallography and mutational studies.
Merceron et al. (2012)