Crystal Structure of activated receptor tyrosine kinase in complex with substrates
The structure was published by Bae, J.H., Lew, E.D., Yuzawa, S., Tome, F., Lax, I., and Schlessinger, J., in 2009 in a paper entitled "The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site." (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.
This PDB entry contains multiple copies of the structure of Basic fibroblast growth factor receptor 1.
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):
This entry contains 1 unique UniProt protein: