3S5Z
Pharmacological Chaperoning in Human alpha-Galactosidase
Summary for 3S5Z
Entry DOI | 10.2210/pdb3s5z/pdb |
Related | 1R46 1R47 3HG2 3HG3 3HG4 3HG5 3S5Y |
Descriptor | Alpha-galactosidase A, beta-D-xylopyranose-(1-2)-[alpha-D-mannopyranose-(1-3)][alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total) |
Functional Keywords | glycoprotein, carbohydrate-binding protein, glycosidase, lysosomal enzyme, (beta/alpha)8 barrel, pharmacological chaperone, hydrolase |
Biological source | Homo sapiens (human) |
Total number of polymer chains | 2 |
Total formula weight | 95196.11 |
Authors | Guce, A.I.,Clark, N.E.,Garman, S.C. (deposition date: 2011-05-23, release date: 2012-01-04, Last modification date: 2023-09-13) |
Primary citation | Guce, A.I.,Clark, N.E.,Rogich, J.J.,Garman, S.C. The molecular basis of pharmacological chaperoning in human alpha-galactosidase Chem.Biol., 18:1521-1526, 2011 Cited by PubMed: 22195554DOI: 10.1016/j.chembiol.2011.10.012 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.001 Å) |
Structure validation
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