Two Classes of p38alpha MAP Kinase Inhibitors Having a Common Diphenylether Core but Exhibiting Divergent Binding Modes
The structure was published by Michelotti, E.L., Moffett, K.K., Nguyen, D., et al., Bukhtiyarova, M., Springman, E.B., and Karpusas, M., in 2005 in a paper entitled "Two classes of p38alpha MAP kinase inhibitors having a common diphenylether core but exhibiting divergent binding modes." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2005.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Mitogen-activated protein kinase 14. This molecule has the UniProt identifier Q16539 (MK14_HUMAN). The sample contained 360 residues which is 100% of the natural sequence. Out of 360 residues 336 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):
This entry contains 1 unique UniProt protein: