PDBe 1a0n

Solution NMR

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

Released:

Function and Biology Details

Reaction catalysed:
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. 
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Tyrosine-protein kinase Fyn Chain: B
Molecule details ›
Chain: B
Length: 69 amino acids
Theoretical weight: 7.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P06241 (Residues: 80-148; Coverage: 13%)
Gene name: FYN
Sequence domains: SH3 domain
Structure domains: SH3 Domains
Phosphatidylinositol 3-kinase regulatory subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 14 amino acids
Theoretical weight: 1.41 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P27986 (Residues: 91-104; Coverage: 2%)
Gene names: GRB1, PIK3R1

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided