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Literature summary extracted from

  • Niefind, K.; Pütter, M.; Guerra, B.; Issinger, O.G.; Schomburg, D.
    GTP plus water mimic ATP in the active site of protein kinase CK2 (1999), Nat. Struct. Biol., 6, 1100-1103.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.1 expression in Escherichia coli Zea mays

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.11.1 the structures of the catalytic subunit of protein kinase CK2 from Zea mays complexed with Mg2+ and with analogs of ATP or GTP are determined to 2.2 A resolution Zea mays

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.1 Zea mays P28523
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.1
-
 Zea mays

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.1 ATP + a protein the enzyme shows dual-cosubstrate specificity because it provides enough space for a hydrogenbonding frame-shift at the nucleotide-binding site and because water molecules allow the purine bases to use the full hydrogen-bonding potential of this site Zea mays ADP + a phosphoprotein
-
 ?
2.7.11.1 GTP + a protein the enzyme shows dual-cosubstrate specificity because it provides enough space for a hydrogenbonding frame-shift at the nucleotide-binding site and because water molecules allow the purine bases to use the full hydrogen-bonding potential of this site Zea mays GDP + a phosphoprotein
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.11.1 heterotetramer
-
 Zea mays

Synonyms

EC Number Synonyms Comment Organism
2.7.11.1 protein kinase CK2
-
 Zea mays