Crystal structure of BTK kinase domain complexed with 2-Methyl-5-[(E)-(3-phenyl-acryloyl)amino]-N-(2-phenyl-3H-imidazo[4,5-b]pyridin-6-yl)-benzamide
The structure was published by Kuglstatter, A., Wong, A., Tsing, S., et al., Shaw, D., Barnett, J.W., and Browner, M.F., in 2011 in a paper entitled "Insights into the conformational flexibility of Bruton's tyrosine kinase from multiple ligand complex structures." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.85 Å and deposited in 2010.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Tyrosine-protein kinase BTK. This molecule has the UniProt identifier Q06187 (BTK_HUMAN). The sample contained 274 residues which is < 90% of the natural sequence. Out of 274 residues 240 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: