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TitleA Novel Organization of Act Domains in Allosteric Enzymes Revealed by the Crystal Structure of Arabidopsis Aspartate Kinase
Journal, issue, pagesPlant Cell, Vol. 18, Page 1681-, Year 2006
Publish dateJan 26, 2006 (structure data deposition date)
AuthorsMas-Droux, C. / Curien, G. / Robert-Genthon, M. / Laurencin, M. / Ferrer, J.L. / Dumas, R.
External linksPlant Cell / PubMed:16731588
MethodsX-ray diffraction
Resolution2.85 Å
Structure data

PDB-2cdq:
Crystal structure of Arabidopsis thaliana aspartate kinase complexed with lysine and S- adenosylmethionine
Method: X-RAY DIFFRACTION / Resolution: 2.85 Å

Chemicals

ChemComp-LYS:
LYSINE

ChemComp-TAR:
D(-)-TARTARIC ACID

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-HOH:
WATER

Source
  • arabidopsis thaliana (thale cress)
KeywordsTRANSFERASE / ASPARTATE KINASE / AMINO ACID METABOLISM / ACT DOMAIN / ALLOSTERY / S-ADENOSYLMETHIONINE / LYSINE / ALLOSTERIC EFFECTOR / PLANT / AMINO ACID BIOSYNTHESIS

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