Crystal structure of MAPKAP kinase 2 (MK2) complexed with a potent 3-aminopyrazole ATP site inhibitor
The structure was published by Velcicky, J., Feifel, R., Hawtin, S., et al., Revesz, L., Scheufler, C., and Schlapbach, A., in 2010 in a paper entitled "Novel 3-aminopyrazole inhibitors of MK-2 discovered by scaffold hopping strategy." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.55 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 299 residues which is < 90% of the natural sequence. Out of 299 residues 284 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: