1mqb Summary

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Crystal Structure of Ephrin A2 (ephA2) Receptor Protein Kinase

The structure was published by Nowakowski, J., Cronin, C.N., McRee, D.E., et al., Scheibe, D.N., Swanson, R.V., and Thompson, D.A., in 2003 in a paper entitled "Structures of the Cancer Related Aurora-A, FAK and EphA2 Protein Kinases from Nanovolume Crystallography" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.3 Å and deposited in 2002.

The experimental data on which the structure is based was not deposited.

This PDB entry contains multiple copies of the structure of Ephrin type-A receptor 2.

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 Ephrin type-A receptor 2 P29317 (596-900) (EPHA2_HUMAN)search Homo sapienssearch < 90% 333 79%
B Ephrin type-A receptor 2 P29317 (596-900) (EPHA2_HUMAN)search Homo sapienssearch < 90% 333 79%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P29317 (596 - 900) Ephrin type-A receptor 2 Homo sapiens

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B Protein kinases, catalytic subunitsearch Phosphorylase Kinase; domain 1search, Transferase(Phosphotransferase) domain 1search Protein tyrosine kinasesearch, Ephrin type-A receptor 2 transmembrane domainsearch

Chain ID Molecular function (GO) Biological process (GO)
A, B (P29317) protein kinase activitysearch protein serine/threonine kinase activitysearch protein tyrosine kinase activitysearch ATP bindingsearch transferase activity, transferring phosphorus-containing groupssearch protein phosphorylationsearch regulation of signal transductionsearch

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