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Structure paper

TitleStructural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains.
Journal, issue, pagesJ. Biol. Chem., Vol. 285, Page 17763-17770, Year 2010
Publish dateFeb 5, 2010 (structure data deposition date)
AuthorsSim, L. / Willemsma, C. / Mohan, S. / Naim, H.Y. / Pinto, B.M. / Rose, D.R.
External linksJ. Biol. Chem. / PubMed:20356844
MethodsX-ray diffraction
Resolution2.15 - 3.2 Å
Structure data

PDB-3lpo:
Crystal structure of the N-terminal domain of sucrase-isomaltase
Method: X-RAY DIFFRACTION / Resolution: 3.2 Å

PDB-3lpp:
Crystal complex of N-terminal sucrase-isomaltase with kotalanol
Method: X-RAY DIFFRACTION / Resolution: 2.15 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-CL:
Unknown entry

ChemComp-BMA:
beta-D-mannopyranose

ChemComp-KTL:
(1S,2R,3R,4S)-1-{(1S)-2-[(2R,3S,4S)-3,4-dihydroxy-2-(hydroxymethyl)tetrahydrothiophenium-1-yl]-1-hydroxyethyl}-2,3,4,5-tetrahydroxypentyl sulfate

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / Glycoside hydrolase family 31 / isomaltase / alpha-glucosidase / Cell membrane / Disease mutation / Disulfide bond / Glycoprotein / Glycosidase / Membrane / Multifunctional enzyme / Polymorphism / Signal-anchor / Sulfation / Transmembrane

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