3r2y Summary


MK2 kinase bound to Compound 1

The structure was published by Barf, T., Kaptein, A., Wilde, S., et al., Hofstra, C., Hornberg, J., and Oubrie, A., in 2011 in a paper entitled "Structure-based lead identification of ATP-competitive MK2 inhibitors." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.0 Å and deposited in 2011.

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

The PDB entry contains the structure of MAP kinase-activated protein kinase 2. This molecule has the UniProt identifier P49137 (MAPK2_HUMAN)search. The sample contained 319 residues which is < 90% of the natural sequence. Out of 319 residues 253 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 MAP kinase-activated protein kinase 2 P49137 (46-364) (MAPK2_HUMAN)search Homo sapienssearch 100% 319 81%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P49137 (46 - 364) MAP kinase-activated protein kinase 2 Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A (P49137) Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search PF00069: Protein kinase domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A (P49137) ATP bindingsearch protein serine/threonine kinase activitysearch transferase activity, transferring phosphorus-containing groupssearch protein kinase activitysearch protein 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 MAP kinase activated protein kinase, C-terminal domainsearch