High resolution crystal structure of mitogen-activated protein kinase-activated protein kinase 3 (MK3)-inhibitor complex
The structure was published by Cheng, R., Felicetti, B., Palan, S., et al., Barker, J., Whittaker, M., and Hesterkamp, T., in 2010 in a paper entitled "High-resolution crystal structure of human Mapkap kinase 3 in complex with a high affinity ligand" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2008.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of MAP kinase-activated protein kinase 3. This molecule has the UniProt identifier Q16644 (MAPK3_HUMAN). The sample contained 336 residues which is < 90% of the natural sequence. Out of 336 residues 272 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: