EGFR-K IN COMPLEX WITH N-[3-[[5-chloro-4-(1H-indol-3-yl)pyrimidin-2-yl]amino]-4-methoxy-phenyl] Prop-2-enamide
The structure was published by Ward, R.A., Anderton, M.J., Ashton, S., et al., Smith, P., Wang, F., and Waring, M.J., in 2013 in a paper entitled "Structure- and Reactivity-Based Development of Covalent Inhibitors of the Activating and Gatekeeper Mutant Forms of the Epidermal Growth Factor Receptor (EGFR)." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.64 Å and deposited in 2013.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of Epidermal growth factor receptor. This molecule has the UniProt identifier P00533 (EGFR_HUMAN). The sample contained 328 residues which is < 90% of the natural sequence. Out of 328 residues 305 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 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: