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TitleStructural basis for the bifunctionality of fructose-1,6-bisphosphate aldolase/phosphatase.
Journal, issue, pagesNature, Vol. 478, Page 538-541, Year 2011
Publish dateMar 10, 2011 (structure data deposition date)
AuthorsFushinobu, S. / Nishimasu, H. / Hattori, D. / Song, H.-J. / Wakagi, T.
External linksNature / PubMed:21983966
MethodsX-ray diffraction
Resolution1.5 Å
Structure data

PDB-3r1m:
Structure of bifunctional fructose 1,6-bisphosphate aldolase/phosphatase (aldolase form)
Method: X-RAY DIFFRACTION / Resolution: 1.5 Å

Chemicals

ChemComp-13P:
1,3-DIHYDROXYACETONEPHOSPHATE

ChemComp-MG:
Unknown entry

ChemComp-MPD:
(4S)-2-METHYL-2,4-PENTANEDIOL / precipitant*YM

ChemComp-HOH:
WATER

Source
  • sulfolobus tokodaii (archaea)
KeywordsMETAL BINDING PROTEIN / Sulfolobus fructose-1 / 6-bisphosphatase-like fold / Hydrolase/aldolase / Mg binding

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