The NMR minimized average structure of the Itk SH2 domain bound to a phosphopeptide
The structure was published by Pletneva, E.V., Sundd, M., Fulton, D.B., and Andreotti, A.H., in 2006 in a paper entitled "Molecular Details of Itk Activation by Prolyl Isomerization and Phospholigand Binding: The NMR Structure of the Itk SH2 Domain Bound to a Phosphopeptide." (abstract).
The structure was determined using NMR spectroscopy and deposited in 2005.
The experimental data on which the structure is based was not deposited.
This PDB entry contains a complex of 2 biomacromolecules, namely Tyrosine-protein kinase ITK/TSK and Lymphocyte cytosolic protein 2 phosphopeptide fragment.
The molecule most likely forms heterodimers.
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 2 unique UniProt proteins: