x-ray crystal structure of 2-aminopyrimidine carbamate 43 bound to Lck
The structure was published by Martin, M.W., Newcomb, J., Nunes, J.J., et al., Johnston, D., Napier, S., and Power, E., in 2006 in a paper entitled "Novel 2-Aminopyrimidine Carbamates as Potent and Orally Active Inhibitors of Lck: Synthesis, SAR, and in Vivo Antiinflammatory Activity" (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2007.
The experimental data on which the structure is based was not 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 273 residues which is < 90% of the natural sequence. Out of 273 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: