1ka6 Summary


SAP/SH2D1A bound to peptide n-pY

The structure was published by Hwang, P.M., Li, C., Morra, M., et al., Pawson, T., Forman-Kay, J.D., and Li, S.C., in 2002 in a paper entitled "A "three-pronged" binding mechanism for the SAP/SH2D1A SH2 domain: structural basis and relevance to the XLP syndrome." (abstract).

The structure was determined using NMR spectroscopy and deposited in 2001.

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

This PDB entry contains a complex of 2 biomacromolecules, namely SH2 DOMAIN PROTEIN 1A and peptide n-pY.

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 SH2 DOMAIN PROTEIN 1A O60880 (1-128) (SH21A_HUMAN)search Homo sapienssearch 100% 128 83%

This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
O60880 (1 - 128) SH2 DOMAIN PROTEIN 1A Homo sapiens
Q13291 (275 - 282) peptide n-pY

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A (O60880) SH2 domainsearch SHC Adaptor Proteinsearch PF00017: SH2 domainsearch

Chain ID Biological process (GO) Molecular function (GO) Cellular component (GO)
A (O60880) cell-cell signalingsearch cellular defense responsesearch positive regulation of natural killer cell mediated cytotoxicitysearch positive regulation of signal transductionsearch humoral immune responsesearch SH3/SH2 adaptor activitysearch protein bindingsearch cytoplasmsearch

Chain InterPro annotation
A SH2 domainsearch SH2 protein 1Asearch