1A0N

NMR STUDY OF THE SH3 DOMAIN FROM FYN PROTO-ONCOGENE TYROSINE KINASE COMPLEXED WITH THE SYNTHETIC PEPTIDE P2L CORRESPONDING TO RESIDUES 91-104 OF THE P85 SUBUNIT OF PI3-KINASE, FAMILY OF 25 STRUCTURES

Summary for 1A0N

DescriptorPRO-PRO-ARG-PRO-LEU-PRO-VAL-ALA-PRO-GLY-SER-SER-LYS-THR, FYN (2 entities in total)
Functional Keywordscomplex (phosphotransferase-peptide), sh3 domain, polyproline-binding, complex (phosphotransferase-peptide) complex, complex (phosphotransferase/peptide)
Biological sourceHomo sapiens (human)
Cellular locationCell membrane P06241
Total number of polymer chains2
Total molecular weight9103.88
Authors
Renzoni, D.A.,Pugh, D.J.R.,Siligardi, G.,Das, P.,Morton, C.J.,Rossi, C.,Waterfield, M.D.,Campbell, I.D.,Ladbury, J.E. (deposition date: 1997-12-05, release date: 1998-02-25, Last modification date: 2011-07-13)
Primary citation
Renzoni, D.A.,Pugh, D.J.,Siligardi, G.,Das, P.,Morton, C.J.,Rossi, C.,Waterfield, M.D.,Campbell, I.D.,Ladbury, J.E.
Structural and thermodynamic characterization of the interaction of the SH3 domain from Fyn with the proline-rich binding site on the p85 subunit of PI3-kinase.
Biochemistry, 35:15646-15653, 1996
PubMed: 8961927 (PDB entries with the same primary citation)
DOI: 10.1021/bi9620969
MImport into Mendeley
Experimental method
SOLUTION NMR
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Structure validation

ClashscoreRamachandran outliersSidechain outliers351.9%24.1%MetricValuePercentile RanksWorseBetterPercentile relative to all structuresPercentile relative to all NMR structures