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Structure paper

TitleCatalytic mechanism of human alpha-galactosidase.
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 3625-3632, Year 2010
Publish dateMay 13, 2009 (structure data deposition date)
AuthorsGuce, A.I. / Clark, N.E. / Salgado, E.N. / Ivanen, D.R. / Kulminskaya, A.A. / Brumer, H. / Garman, S.C.
External linksJ. Biol. Chem. / PubMed:19940122
MethodsX-ray diffraction
Resolution1.9 - 2.3 Å
Structure data

PDB-3hg2:
Human alpha-galactosidase catalytic mechanism 1. Empty active site
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3hg3:
Human alpha-galactosidase catalytic mechanism 2. Substrate bound
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

PDB-3hg4:
Human alpha-galactosidase catalytic mechanism 3. Covalent intermediate
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-3hg5:
Human alpha-galactosidase catalytic mechanism 4. Product bound
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-SO4:
SULFATE ION

ChemComp-ACY:
ACETIC ACID

ChemComp-GAL:
beta-D-galactopyranose

ChemComp-HOH:
WATER

ChemComp-2PE:
NONAETHYLENE GLYCOL / precipitant*YM

ChemComp-7JZ:
2-deoxy-2,2-difluoro-beta-D-lyxo-hexopyranose

ChemComp-GLA:
alpha-D-galactopyranose

Source
  • homo sapiens (human)
KeywordsHYDROLASE / GLYCOPROTEIN / CARBOHYDRATE-BINDING PROTEIN / GLYCOSIDASE / LYSOSOMAL ENZYME / (BETA/ALPHA)8 BARREL / Disease mutation / Disulfide bond / Lysosome

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