2jiv Summary

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Crystal structure of EGFR kinase domain T790M mutation in compex with HKI-272

The structure was published by Yun, C.-H., Mengwasser, K.E., Toms, A.V., et al., Wong, K.-K., Meyerson, M., and Eck, M.J., in 2008 in a paper entitled "The T790M Mutation in Egfr Kinase Causes Drug Resistance by Increasing the Affinity for ATP." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.5 Å and deposited in 2007.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of EPIDERMAL 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):


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 (695-1022) (EGFR_HUMAN)search Homo sapienssearch < 90% 328 82%
B EPIDERMAL GROWTH FACTOR RECEPTOR P00533 (695-1022) (EGFR_HUMAN)search Homo sapienssearch < 90% 328 82%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00533 (695 - 1022) EPIDERMAL GROWTH FACTOR RECEPTOR Homo sapiens

Chain Structural classification (CATH) Sequence family (Pfam)
A, B Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search Protein tyrosine kinasesearch

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

Chain InterPro annotation
A, B 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