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Structure paper

TitleThe molecular basis of pharmacological chaperoning in human alpha-galactosidase
Journal, issue, pagesChem. Biol., Vol. 18, Page 1521-1526, Year 2011
Publish dateMay 23, 2011 (structure data deposition date)
AuthorsGuce, A.I. / Clark, N.E. / Rogich, J.J. / Garman, S.C.
External linksChem. Biol. / PubMed:22195554
MethodsX-ray diffraction
Resolution2.001 - 2.639 Å
Structure data

PDB-3s5y:
Pharmacological Chaperoning in Human alpha-Galactosidase
Method: X-RAY DIFFRACTION / Resolution: 2.105 Å

PDB-3s5z:
Pharmacological Chaperoning in Human alpha-Galactosidase
Method: X-RAY DIFFRACTION / Resolution: 2.001 Å

PDB-3tv8:
Pharmacological Chaperoning in Human alpha-Galactosidase
Method: X-RAY DIFFRACTION / Resolution: 2.639 Å

Chemicals

ChemComp-DGJ:
(2R,3S,4R,5S)-2-(hydroxymethyl)piperidine-3,4,5-triol / medication, Galafold*YM

ChemComp-2PE:
NONAETHYLENE GLYCOL / precipitant*YM

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

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-ACY:
ACETIC ACID

ChemComp-HOH:
WATER

ChemComp-GLA:
alpha-D-galactopyranose

ChemComp-GAL:
beta-D-galactopyranose

ChemComp-GOL:
GLYCEROL

ChemComp-SO4:
SULFATE ION

Source
  • homo sapiens (human)
KeywordsHYDROLASE/HYDROLASE INHIBITOR / glycoprotein / carbohydrate-binding protein / glycosidase / lysosomal enzyme / (beta/alpha)8 barrel / pharmacological chaperone / HYDROLASE-HYDROLASE INHIBITOR complex / HYDROLASE / n-linked glycosylation / lysosome

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