3EQA
Catalytic domain of glucoamylase from aspergillus niger complexed with tris and glycerol
Summary for 3EQA
Entry DOI | 10.2210/pdb3eqa/pdb |
Descriptor | Glucoamylase, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
Functional Keywords | hydrolase, glycoprotein, glycosidase, polysaccharide degradation |
Biological source | Aspergillus Niger |
Total number of polymer chains | 1 |
Total formula weight | 54122.08 |
Authors | Lee, J.,Paetzel, M. (deposition date: 2008-09-30, release date: 2009-10-13, Last modification date: 2023-09-06) |
Primary citation | Lee, J.,Paetzel, M. Structure of the catalytic domain of glucoamylase from Aspergillus niger. Acta Crystallogr.,Sect.F, 67:188-192, 2011 Cited by PubMed: 21301084DOI: 10.1107/S1744309110049390 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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