Crystal structure of p38 kinase bound to pyrimido-pyridazinone inhibitor
The structure was published by Pearlman, D.A., in 2005 in a paper entitled "Evaluating the molecular mechanics poisson-boltzmann surface area free energy method using a congeneric series of ligands to p38 MAP kinase." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2008.
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 B4E0K5 (B4E0K5_HUMAN). The sample contained 366 residues which is 100% of the natural sequence. Out of 366 residues 329 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: