Crystal structure of the catalytic domain of c-Met kinase in complex with ARQ 197
The structure was published by Eathiraj, S., Palma, R., Volckova, E., et al., France, D.S., Ashwell, M.A., and Chan, T.C., in 2011 in a paper entitled "Discovery of a novel mode of protein kinase inhibition characterized by the mechanism of inhibition of human mesenchymal-epithelial transition factor (c-Met) protein autophosphorylation by ARQ 197." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 1.94 Å and deposited in 2011.
The experimental data on which the structure is based was also deposited.
This PDB entry contains multiple copies of the structure of Hepatocyte growth factor receptor.
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 has more than one probable quaternary state observed. For more details see the quaternary structure page.
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: