Crystal structure of an optimzied benzothiophene inhibitor bound to MAPKAP Kinase-2 (MK-2)
The structure was published by Anderson, D.R., Meyers, M.J., Kurumbail, R.G., et al., Mahoney, M.W., Mourey, R.J., and Parikh, M.D., in 2009 in a paper entitled "Benzothiophene inhibitors of MK2. Part 2: improvements in kinase selectivity and cell potency." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 3.8 Å and deposited in 2009.
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). The sample contained 327 residues which is < 90% of the natural sequence. Out of 327 residues 282 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 has more than one probable quaternary state observed. For more details see the quaternary structure page.
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):
This entry contains 1 unique UniProt protein: