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TitleEvolved to Be Active: Sulfate Ions Define Substrate Recognition Sites of CK2alpha and Emphasise its Exceptional Role within the CMGC Family of Eukaryotic Protein Kinases
Journal, issue, pagesJ. Mol. Biol., Vol. 370, Page 427-438, Year 2007
Publish dateMay 10, 2007 (structure data deposition date)
AuthorsNiefind, K. / Yde, C.W. / Ermakova, I. / Issinger, O.G.
External linksJ. Mol. Biol. / PubMed:17524418
MethodsX-ray diffraction
Resolution1.605 Å
Structure data

PDB-2pvr:
Crystal structure of the catalytic subunit of protein kinase CK2 (C-terminal deletion mutant 1-335) in complex with two sulfate ions
Method: X-RAY DIFFRACTION / Resolution: 1.605 Å

Chemicals

ChemComp-SO4:
SULFATE ION

ChemComp-ANP:
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / AMP-PNP, energy-carrying molecule analogue*YM

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / TRANSFERASE / EUKARYOTIC PROTEIN KINASE FOLD / CMGC kinases

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