Crystal structure of a binary complex of the catalytic subunit of protein kinase CK2 with Mg-AMPPNP
The structure was published by Yde, C.W., Ermakova, I., Issinger, O.G., and Niefind, K., in 2005 in a paper entitled "Inclining the purine base binding plane in protein kinase CK2 by exchanging the flanking side-chains generates a preference for ATP as a cosubstrate." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.86 Å and deposited in 2002.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Protein kinase CK2. This molecule has the UniProt identifier P28523 (CSK2A_MAIZE). The sample contained 332 residues which is 100% of the natural sequence. Out of 332 residues 327 were observed and are deposited in the PDB.
It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.
The molecule is most likely monomeric.
The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):
This entry contains 1 unique UniProt protein: