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CRYSTAL STRUCTURE OF A BINARY COMPLEX OF PROTEIN KINASE CK2 (ALPHA-SUBUNIT) AND MG-GMPPNP

The structure was published by Niefind, K., Putter, M., Guerra, B., Issinger, O.G., and Schomburg, D., in 1999 in a paper entitled "GTP plus water mimic ATP in the active site of protein kinase CK2." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.2 Å and deposited in 1999.

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)search. The sample contained 327 residues which is 98% of the natural sequence. Out of 327 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):


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 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) PROTEIN KINASE CK2 Zea mays

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

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