› 2xn0

X-ray diffraction
2.5Å resolution

Structure of alpha-galactosidase from Lactobacillus acidophilus NCFM, PtCl4 derivative

Released:
DOI: 10.2210/pdb2xn0/pdb
PDB entry 2xn0 coloured by chain, front view.
PDB entry 2xn0 coloured by chain, side view.
PDB entry 2xn0 coloured by chain, top view.
Source organism: Lactobacillus acidophilus NCFM
Primary publication:
Crystal structure of α-galactosidase from Lactobacillus acidophilus NCFM: insight into tetramer formation and substrate binding.
Fredslund F, Hachem MA, Larsen RJ, Sørensen PG, Coutinho PM, Lo Leggio L, Svensson B
J Mol Biol 412 466-80 (2011)
PMID: 21827767

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-124228 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-galactosidase Mel36A Chains: A, B
Molecule details ›
Chains: A, B
Length: 732 amino acids
Theoretical weight: 84.59 KDa
Source organism: Lactobacillus acidophilus NCFM
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: G1UB44 (Residues: 1-732; Coverage: 100%)
Gene names: LBA1438, aga, melA
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand PT 17 x PT
Ligand GOL 13 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P21212
Unit cell:
a: 126.37Å b: 149.58Å c: 90.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.15 0.148 0.203
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

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

3 mentions without citation

α-Galactosidase/sucrose kinase (AgaSK), a novel bifunctional enzyme from the human microbiome coupling galactosidase and kinase activities.
Bruel et al. (2011)
2 more