1zoh Summary

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Crystal structure of protein kinase CK2 in complex with TBB-derivatives inhibitors

The structure was published by Battistutta, R., Mazzorana, M., Sarno, S., Kazimierczuk, Z., Zanotti, G., and Pinna, L.A., in 2005 in a paper entitled "Inspecting the structure-activity relationship of protein kinase CK2 inhibitors derived from tetrabromo-benzimidazole." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.81 Å and deposited in 2005.

The experimental data on which the structure is based was not deposited.

The PDB entry contains the structure of PROTEIN KINASE CK2, ALPHA SUBUNIT. This molecule has the UniProt identifier P28523 (CSK2A_MAIZE)search. The sample contained 332 residues which is 100% of the natural sequence. Out of 332 residues 325 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 most likely forms homodimers.

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 PROTEIN KINASE CK2, ALPHA SUBUNIT P28523 (1-332) (CSK2A_MAIZE)search Zea mayssearch 98% 332 98%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P28523 (1 - 332) PROTEIN KINASE CK2, ALPHA SUBUNIT Zea mays

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

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

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