3A5V
Crystal structure of alpha-galactosidase I from Mortierella vinacea
Summary for 3A5V
| Entry DOI | 10.2210/pdb3a5v/pdb |
| Descriptor | Alpha-galactosidase, alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]alpha-D-mannopyranose-(1-6)-[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, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (7 entities in total) |
| Functional Keywords | beta/alpha barrel, n-glycosylation, hydrolase |
| Biological source | Umbelopsis vinacea |
| Total number of polymer chains | 1 |
| Total formula weight | 47322.66 |
| Authors | Fujimoto, Z.,Kaneko, S.,Kobayashi, H. (deposition date: 2009-08-12, release date: 2009-08-25, Last modification date: 2024-11-20) |
| Primary citation | Fujimoto, Z.,Kaneko, S.,Kim, W.-D.,Park, G.-G.,Momma, M.,Kobayashi, H. The Tetramer Structure of the Glycoside Hydrolase Family 27 alpha-Galactosidase I from Umbelopsis vinacea Biosci.Biotechnol.Biochem., 73:2360-2364, 2009 Cited by PubMed Abstract: The crystal structure of Umbelopsis vinacea alpha-galactosidase I, which belongs to glycoside hydrolase family 27, was determined at 2.0 A resolution. The monomer structure was well conserved with those of glycoside hydrolase family 27 enzymes. The biological tetramer structure of this enzyme was constructed by the crystallographic 4-fold symmetry, and tetramerization appeared to be caused by three inserted peptides that were involved in the tetramer interface. The quaternary structure indicated that the substrate specificity of this enzyme might be related to the tetramer formation. Three N-glycosylated sugar chains were observed, and their structures were found to be of the high-mannose type. PubMed: 19809163DOI: 10.1271/bbb.90604 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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