CRYSTALLOGRAPHIC STUDIES OF AN ACTIVATION LOOP MUTANT OF THE INSULIN RECEPTOR TYROSINE KINASE
The structure was published by Till, J.H., Ablooglu, A.J., Frankel, M., Bishop, S.M., Kohanski, R.A., and Hubbard, S.R., in 2001 in a paper entitled "Crystallographic and solution studies of an activation loop mutant of the insulin receptor tyrosine kinase: insights into kinase mechanism." (abstract).
This crystal structure was determined using X-ray diffraction at a resolution of 2.4 Å and deposited in 2001.
The experimental data on which the structure is based was also deposited.
The PDB entry contains the structure of INSULIN RECEPTOR. This molecule has the UniProt identifier P06213 (INSR_HUMAN). The sample contained 306 residues which is < 90% of the natural sequence. Out of 306 residues 278 were observed and are deposited in the PDB.
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 is most likely monomeric.
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: