› 3lrm

X-ray diffraction
2.7Å resolution

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-138199 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Alpha-galactosidase 1 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 479 amino acids
Theoretical weight: 53.08 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Saccharomyces cerevisiae
UniProt:
  • Canonical: P04824 (Residues: 1-471; Coverage: 100%)
Gene name: MEL1
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
Carbohydrate polymer : NEW Components: GLC, FRU, GLA
Carbohydrate polymer
1 bound ligand:
Ligand NAG 9 x NAG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P212121
Unit cell:
a: 111.17Å b: 129.53Å c: 136.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.243 0.241 0.284
Expression system: Saccharomyces cerevisiae

Quick links

Citations

3 review citations

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

3 mentions without citation

Functional analysis of family GH36 α-galactosidases from Ruminococcus gnavus E1: insights into the metabolism of a plant oligosaccharide by a human gut symbiont.
Cervera-Tison et al. (2012)
2 more