2eb2 Summary

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Crystal structure of mutated EGFR kinase domain (G719S)

The structure was published by Yoshikawa, S., Kukimoto-Niino, M., Parker, L., et al., Semba, K., Yamamoto, T., and Yokoyama, S., in 2012 in a paper entitled "Structural basis for the altered drug sensitivities of non-small cell lung cancer-associated mutants of human epidermal growth factor receptor" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.5 Å and deposited in 2007.

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 334 residues which is < 90% of the natural sequence. Out of 334 residues 305 were observed and are deposited in the PDB.

The molecule most likely forms homodimers.

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% 334 91%


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 Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search Protein tyrosine kinasesearch

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

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