› 3hg2

X-ray diffraction
2.3Å resolution

Human alpha-galactosidase catalytic mechanism 1. Empty active site

Released:
DOI: 10.2210/pdb3hg2/pdb
PDB entry 3hg2 coloured by chain, front view.
PDB entry 3hg2 coloured by chain, side view.
PDB entry 3hg2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Catalytic mechanism of human alpha-galactosidase.
Guce AI, Clark NE, Salgado EN, Ivanen DR, Kulminskaya AA, Brumer H, Garman SC
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
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 (3 distinct):
Alpha-galactosidase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 398 amino acids
Theoretical weight: 45.39 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
  • Canonical: P06280 (Residues: 32-429; Coverage: 100%)
Gene name: GLA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG, FUC
Carbohydrate polymer
Carbohydrate polymer : NEW Components: NAG, BMA
Carbohydrate polymer
4 bound ligands:
Ligand NAG 3 x NAG
Ligand SO4 3 x SO4
Ligand ACY 3 x ACY
Ligand GAL 1 x GAL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P3221
Unit cell:
a: 90.813Å b: 90.813Å c: 217.166Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.178 0.176 0.202
Expression system: Homo sapiens

Quick links

Citations

17 review citations

Fabry disease.
Germain DP. (2010)
16 more

2 mentions without citation

Catalytic mechanism of human alpha-galactosidase.
Guce et al. (2010)
1 more