2jyq Summary

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NMR structure of the apo v-Src SH2 domain

The structure was published by Taylor, J.D., Ababou, A., Fawaz, R.R., Hobbs, C.J., Williams, M.A., and Ladbury, J.E., in 2008 in a paper entitled "Structure, dynamics, and binding thermodynamics of the v-Src SH2 domain: Implications for drug design" (abstract).

The structure was determined using NMR spectroscopy and deposited in 2007.

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

The PDB entry contains the structure of Tyrosine-protein kinase transforming protein Src. This molecule has the UniProt identifier P63185 (SRC_RSVSE)search. The sample contained 106 residues which is < 90% of the natural sequence. Out of 106 residues 106 were observed and are deposited in the PDB.

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 transforming protein Src P63185 (144-249) (SRC_RSVSE)search Rous sarcoma virus (strain Schmidt-Ruppin E)search < 90% 106 100%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P63185 (144 - 249) Tyrosine-protein kinase transforming protein Src Rous sarcoma virus

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