1lr4 Summary

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PDB entry 1lr4 (supersedes 1a6o)

Room Temperature Crystal Structure of the Apo-form of the catalytic subunit of protein kinase CK2 from Zea mays

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 2.0 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)search. 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):


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 (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 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) protein serine/threonine kinase activitysearch ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein kinase activitysearch kinase activitysearch transferase activitysearch nucleotide bindingsearch 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