› 3hg2

X-ray diffraction
2.3Å resolution

Human alpha-galactosidase catalytic mechanism 1. Empty active site

Released:
DOI: 10.2210/pdb3hg2/pdb
PDB 3hg2 coloured by chain and viewed from the front.
PDB 3hg2 coloured by chain and viewed from the side.
PDB 3hg2 coloured by chain and viewed from the top.
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

Reactions catalysed: 
Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids
Alpha-D-galactosyl-(1->4)-beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide + H(2)O = D-galactose + beta-D-galactosyl-(1->4)-beta-D-glucosyl-(1<->1)-ceramide
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (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

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Citations

12 review citations

Acute Intermittent Porphyria: An Overview of Therapy Developments and Future Perspectives Focusing on Stabilisation of HMBS and Proteostasis Regulators.
Bustad et al. (2021)
11 more

2 mentions without citation

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