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Structure paper

TitleA conserved glutamate residue exhibits multifunctional catalytic roles in D-fructose-1,6-bisphosphate aldolases.
Journal, issue, pagesJ. Biol. Chem., Vol. 277, Page 9474-9483, Year 2002
Publish dateApr 25, 2000 (structure data deposition date)
AuthorsMAURADY, A. / ZDANOV, A. / De Moissac, D. / Beaudry, D. / SYGUSCH, J.
External linksJ. Biol. Chem. / PubMed:11779856
MethodsX-ray diffraction
Resolution2 - 2.6 Å
Structure data

PDB-1ewd:
FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE
Method: X-RAY DIFFRACTION / Resolution: 2.464 Å

PDB-1ewe:
Fructose 1,6-Bisphosphate Aldolase from Rabbit Muscle
Method: X-RAY DIFFRACTION / Resolution: 2.6 Å

PDB-1ex5:
FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE FROM RABBIT MUSCLE
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-3b8d:
Fructose 1,6-bisphosphate aldolase from rabbit muscle
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-SO4:
SULFATE ION

Source
  • oryctolagus cuniculus (rabbit)
KeywordsLYASE / ALDOLASE / SCHIFF BASE / LYASE(ALDEHYDE) / GLYCOLISIS / ALPHA/BETA BARREL / GLYCOLYSIS / Acetylation / Phosphorylation

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