2eu0 Summary


The NMR ensemble 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):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Tyrosine-protein kinase ITK/TSK Q03526 (238-344) (ITK_MOUSE)search Mus musculussearch < 90% 109 100%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
Q03526 (238 - 344) Tyrosine-protein kinase ITK/TSK Mus musculus
Q60787 (143 - 148) Lymphocyte cytosolic protein 2 phosphopeptide fragment

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A SH2 domainsearch SHC Adaptor Proteinsearch SH2 domainsearch
Chain InterPro annotation
A SH2 domainsearch