› 1pic

Solution NMR

PHOSPHATIDYLINOSITOL 3-KINASE, P85-ALPHA SUBUNIT: C-TERMINAL SH2 DOMAIN COMPLEXED WITH A TYR751 PHOSPHOPEPTIDE FROM THE PDGF RECEPTOR, NMR, MINIMIZED MEAN STRUCTURE

Released:
DOI: 10.2210/pdb1pic/pdb
PDB entry 1pic coloured by chain, front view.
PDB entry 1pic coloured by chain, side view.
PDB entry 1pic coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of a specific peptide complex of the carboxy-terminal SH2 domain from the p85 alpha subunit of phosphatidylinositol 3-kinase.
Breeze AL, Kara BV, Barratt DG, Anderson M, Smith JC, Luke RW, Best JR, Cartlidge SA
EMBO J 15 3579-89 (1996)
PMID: 8670861

Function and Biology Details

Reaction catalysed: 
ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151136 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phosphatidylinositol 3-kinase regulatory subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 12.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P27986 (Residues: 616-724; Coverage: 15%)
Gene names: GRB1, PIK3R1
Sequence domains: SH2 domain
Structure domains: SH2 domain
BETA-PLATELET-DERIVED GROWTH FACTOR RECEPTOR Chain: B
Molecule details ›
Chain: B
Length: 6 amino acids
Theoretical weight: 728 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

3 review citations

Structure and function of phosphoinositide 3-kinases.
Wymann et al. (1998)
2 more

4 mentions without citation

Somatic mutations in PI3Kalpha: structural basis for enzyme activation and drug design.
Gabelli et al. (2010)
3 more