3gop Summary

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Crystal structure of the EGF receptor juxtamembrane and kinase domains

The structure was published by Red Brewer, M., Choi, S.H., Alvarado, D., et al., Pozzi, A., Lemmon, M.A., and Carpenter, G., in 2009 in a paper entitled "The juxtamembrane region of the EGF receptor functions as an activation domain." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 2009.

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 361 residues which is < 90% of the natural sequence. Out of 361 residues 294 were observed and are deposited in the PDB.

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 (669-1022) (EGFR_HUMAN)search Homo sapienssearch < 90% 361 83%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P00533 (669 - 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 ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein tyrosine kinase activitysearch 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