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Structure paper

TitleThe structure of barley alpha-amylase isozyme 1 reveals a novel role of domain C in substrate recognition and binding: a pair of sugar tongs
Journal, issue, pagesStructure, Vol. 11, Page 973-984, Year 2003
Publish dateDec 29, 2000 (structure data deposition date)
AuthorsRobert, X. / Haser, R. / Gottschalk, T.E. / Ratajczak, F. / Driguez, H. / Svensson, B. / Aghajari, N.
External linksStructure / PubMed:12906828
MethodsX-ray diffraction
Resolution1.5 - 2 Å
Structure data

PDB-1ht6:
CRYSTAL STRUCTURE AT 1.5A RESOLUTION OF THE BARLEY ALPHA-AMYLASE ISOZYME 1
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

PDB-1p6w:
Crystal structure of barley alpha-amylase isozyme 1 (AMY1) in complex with the substrate analogue, methyl 4I,4II,4III-tri-thiomaltotetraoside (thio-DP4)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-CA:
Unknown entry

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-HOH:
WATER

Source
  • hordeum vulgare (barley)
KeywordsHYDROLASE / BARLEY / ALPHA-AMYLASE / ISOZYME 1 / BETA-ALPHA-BARREL / SUGAR TONGS BINDING SITE / SUBSTRATE ANALOGUE

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