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: 21301084 DOI: 10.1107/S1744309110049390 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.9 Å)

Structure validation