3hg3

X-ray diffraction
1.9Å resolution

Human alpha-galactosidase catalytic mechanism 2. Substrate bound

Released:
Source organism: Homo sapiens
Primary publication:
Catalytic mechanism of human alpha-galactosidase.
J Biol Chem 285 3625-3632 (2010)
PMID: 19940122

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

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: 46.18 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 : NEW Components: NAG
Carbohydrate polymer : NEW Components: GLC, GLA
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 59.548Å b: 106.106Å c: 181.721Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.165 0.197
Expression system: Trichoplusia ni