4hcu Summary

pdbe.org/4hcu
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Crystal structure of ITK in complext with compound 40

The structure was published by Zapf, C.W., Gerstenberger, B.S., Xing, L., et al., Czerwinski, R.M., Seth, N., and Medley, Q.G., in 2012 in a paper entitled "Covalent inhibitors of interleukin-2 inducible T cell kinase (itk) with nanomolar potency in a whole-blood assay." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 1.43 Å and deposited in 2012.

The experimental data on which the structure is based was also deposited.

The PDB entry contains the structure of Tyrosine-protein kinase ITK/TSK. This molecule has the UniProt identifier Q08881 (ITK_HUMAN)search. The sample contained 269 residues which is < 90% of the natural sequence. Out of 269 residues 263 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):


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 Q08881 (354-620) (ITK_HUMAN)search Homo sapienssearch < 90% 269 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q08881 (354 - 620) Tyrosine-protein kinase ITK/TSK Homo sapiens

Chain Sequence family (Pfam)
A Protein tyrosine kinasesearch

Chain ID Biological process (GO) Molecular function (GO)
A (Q08881) protein phosphorylationsearch transferase activity, transferring phosphorus-containing groupssearch protein kinase activitysearch ATP bindingsearch protein tyrosine kinase activitysearch

Chain InterPro annotation
A 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