3kxh Summary


Crystal structure of Z. mays CK2 kinase alpha subunit in complex with the inhibitor (2-dymethylammino-4,5,6,7-tetrabromobenzoimidazol-1yl-acetic acid (K66)

The structure was published by Sarno, S., Papinutto, E., Franchin, C., et al., Zanotti, G., Battistutta, R., and Pinna, L.A., in 2011 in a paper entitled "ATP site-directed inhibitors of protein kinase CK2: an update." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.7 Å and deposited in 2009.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Casein kinase II subunit alpha. This molecule has the UniProt identifier P28523 (CSK2A_MAIZE)search. The sample contained 327 residues which is 98% of the natural sequence. Out of 327 residues 326 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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Casein kinase II subunit alpha P28523 (2-328) (CSK2A_MAIZE)search Zea mayssearch 98% 327 100%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P28523 (2 - 328) Casein kinase II subunit alpha Zea mays

Chain Structural classification (CATH) Sequence family (Pfam)
A (P28523) Transferase(Phosphotransferase) domain 1search, Phosphorylase Kinase; domain 1search PF00069: Protein kinase domainsearch

Chain ID Biological process (GO) Molecular function (GO)
A (P28523) protein phosphorylationsearch phosphorylationsearch protein kinase activitysearch ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein serine/threonine kinase activitysearch kinase activitysearch transferase activitysearch nucleotide bindingsearch

Chain InterPro annotation
A Protein kinase domainsearch Serine/threonine/dual specificity protein kinase, catalytic domainsearch Serine/threonine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch