Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Zea mays |
Crystallization (Comment) | Organism |
---|---|
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 | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | P28523 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Zea mays |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
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 | - |
? | |
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 | Comment | Organism |
---|---|---|
heterotetramer | - |
Zea mays |
Synonyms | Comment | Organism |
---|---|---|
protein kinase CK2 | - |
Zea mays |