3LPO
Crystal structure of the N-terminal domain of sucrase-isomaltase
Summary for 3LPO
Entry DOI | 10.2210/pdb3lpo/pdb |
Related | 3LPP |
Descriptor | Sucrase-isomaltase, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 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, ... (4 entities in total) |
Functional Keywords | glycoside hydrolase family 31, isomaltase, alpha-glucosidase, cell membrane, disease mutation, disulfide bond, glycoprotein, glycosidase, hydrolase, membrane, multifunctional enzyme, polymorphism, signal-anchor, sulfation, transmembrane |
Biological source | Homo sapiens (human) |
Cellular location | Apical cell membrane; Single-pass type II membrane protein: P14410 |
Total number of polymer chains | 4 |
Total formula weight | 415245.08 |
Authors | Sim, L.,Rose, D.R. (deposition date: 2010-02-05, release date: 2010-03-31, Last modification date: 2020-07-29) |
Primary citation | Sim, L.,Willemsma, C.,Mohan, S.,Naim, H.Y.,Pinto, B.M.,Rose, D.R. Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains. J.Biol.Chem., 285:17763-17770, 2010 Cited by PubMed: 20356844DOI: 10.1074/jbc.M109.078980 PDB entries with the same primary citation |
Experimental method |
Structure validation
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