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-Structure paper
Title | Structural basis for substrate selectivity in human maltase-glucoamylase and sucrase-isomaltase N-terminal domains. |
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Journal, issue, pages | J. Biol. Chem., Vol. 285, Page 17763-17770, Year 2010 |
Publish date | Feb 5, 2010 (structure data deposition date) |
Authors | Sim, L. / Willemsma, C. / Mohan, S. / Naim, H.Y. / Pinto, B.M. / Rose, D.R. |
External links | J. Biol. Chem. / PubMed:20356844 |
Methods | X-ray diffraction |
Resolution | 2.15 - 3.2 Å |
Structure data | PDB-3lpo: PDB-3lpp: |
Chemicals | ChemComp-NAG: ChemComp-TRS: ChemComp-PEG: ChemComp-CL: ChemComp-BMA: ChemComp-KTL: ChemComp-HOH: |
Source |
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Keywords | HYDROLASE / Glycoside hydrolase family 31 / isomaltase / alpha-glucosidase / Cell membrane / Disease mutation / Disulfide bond / Glycoprotein / Glycosidase / Membrane / Multifunctional enzyme / Polymorphism / Signal-anchor / Sulfation / Transmembrane |