4li5 Summary


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)search. 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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Epidermal growth factor receptor P00533 (696-1020) (EGFR_HUMAN)search Homo sapienssearch < 90% 328 93%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00533 (696 - 1020) Epidermal growth factor receptor Homo sapiens

Chain Sequence family (Pfam)
A Protein tyrosine kinasesearch

Chain ID Biological process (GO) Molecular function (GO)
A (P00533) protein phosphorylationsearch protein kinase activitysearch ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein tyrosine kinase activitysearch

Chain InterPro annotation
A Protein kinase domainsearch Serine-threonine/tyrosine-protein kinase catalytic domainsearch Tyrosine-protein kinase, active sitesearch Protein kinase-like domainsearch Protein kinase, ATP binding sitesearch Tyrosine-protein kinase, catalytic domainsearch