Crystal structure of imidazo quinoxaline 1 bound to the kinase domain of human LCK, activated form (auto-phosphorylated on TYR394)
The structure was published by Ozawa, T., Tsuji, E., Ozawa, M., et al., Nishimura, T., Kobayashi, S., and Okazaki, K., in 2008 in a paper entitled "The importance of CH/pi hydrogen bonds in rational drug design: An ab initio fragment molecular orbital study to leukocyte-specific protein tyrosine (LCK) kinase" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.7 Å and deposited in 2008.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Proto-oncogene tyrosine-protein kinase LCK. This molecule has the UniProt identifier P06239 (LCK_HUMAN). The sample contained 285 residues which is < 90% of the natural sequence. Out of 285 residues 271 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: