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; PubMed: 20356844; DOI: 10.1074/jbc.M109.078980

Experimental method

X-RAY DIFFRACTION (3.2 Å)