P38 in complex with Imatinib
The structure was published by Namboodiri, H.V., Bukhtiyarova, M., Ramcharan, J., Karpusas, M., Lee, Y., and Springman, E.B., in 2010 in a paper entitled "Analysis of imatinib and sorafenib binding to p38alpha compared with c-Abl and b-Raf provides structural insights for understanding the selectivity of inhibitors targeting the DFG-out form of protein kinases." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2009.
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 348 residues which is 97% of the natural sequence. Out of 348 residues 328 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: