› 3lx9

X-ray diffraction
2.04Å resolution

Interconversion of Human Lysosomal Enzyme Specificities

Released:
DOI: 10.2210/pdb3lx9/pdb
PDB entry 3lx9 coloured by chain, front view.
PDB entry 3lx9 coloured by chain, side view.
PDB entry 3lx9 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Interconversion of the specificities of human lysosomal enzymes associated with Fabry and Schindler diseases.
Tomasic IB, Metcalf MC, Guce AI, Clark NE, Garman SC
J Biol Chem 285 21560-6 (2010)
PMID: 20444686

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:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138990 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (4 distinct):
Alpha-galactosidase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 404 amino acids
Theoretical weight: 46.14 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P06280 (Residues: 32-429; Coverage: 100%)
Gene name: GLA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, BMA, MAN
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA, MAN, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
2 bound ligands:
Ligand NAG 2 x NAG
Ligand A2G 2 x A2G
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: C2221
Unit cell:
a: 89.947Å b: 139.492Å c: 182.58Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.178 0.176 0.218
Expression system: Trichoplusia ni

Quick links

Citations

3 review citations

Fabry disease.
Germain DP. (2010)
2 more

3 mentions without citation

Coupling Protein Side-Chain and Backbone Flexibility Improves the Re-design of Protein-Ligand Specificity.
Ollikainen et al. (2015)
2 more