Crystal structure of PYK2 complexed with PF-431396
The structure was published by Han, S., Mistry, A., Chang, J.S., et al., Walker, D.P., Brosius, A.D., and Buckbinder, L., in 2009 in a paper entitled "Structural characterization of proline-rich tyrosine kinase 2 (PYK2) reveals a unique (DFG-out) conformation and enables inhibitor design." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2009.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Protein tyrosine kinase 2 beta. This molecule has the UniProt identifier Q14289 (FAK2_HUMAN). The sample contained 277 residues which is < 90% of the natural sequence. Out of 277 residues 261 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: