1aou Summary

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NMR STRUCTURE OF THE FYN SH2 DOMAIN COMPLEXED WITH A PHOSPHOTYROSYL PEPTIDE, 22 STRUCTURES

The structure was published by Mulhern, T.D., Shaw, G.L., Morton, C.J., Day, A.J., and Campbell, I.D., in 1997 in a paper entitled "The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity." (abstract).

The structure was determined using NMR spectroscopy and deposited in 1997.

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

This PDB entry contains a complex of 2 biomacromolecules, namely FYN PROTEIN-TYROSINE KINASE and PHOSPHOTYROSYL PEPTIDE.

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
F FYN PROTEIN-TYROSINE KINASE P06241 (143-248) (FYN_HUMAN)search Homo sapienssearch < 90% 106 100%
P PHOSPHOTYROSYL PEPTIDE P03079 (321-331) (MT_POVHA)search Hamster polyomavirussearch < 90% 11 100%


This entry contains 2 unique UniProt proteins:

UniProt accession Name Organism PDB
P06241 (143 - 248) FYN PROTEIN-TYROSINE KINASE Homo sapiens
P03079 (321 - 331) PHOSPHOTYROSYL PEPTIDE Hamster polyomavirus

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