› 1oo3

Solution NMR

P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase

Released:
DOI: 10.2210/pdb1oo3/pdb
PDB entry 1oo3 coloured by chain, front view.
PDB entry 1oo3 coloured by chain, side view.
PDB entry 1oo3 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Nuclear magnetic resonance structure of the P395S mutant of the N-SH2 domain of the p85 subunit of PI3 kinase: an SH2 domain with altered specificity.
Günther UL, Weyrauch B, Zhang X, Schaffhausen B
Biochemistry 42 11120-7 (2003)
PMID: 14503862

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150051 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylinositol 3-kinase regulatory subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 111 amino acids
Theoretical weight: 12.86 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P23727 (Residues: 321-431; Coverage: 15%)
Gene name: PIK3R1
Sequence domains: SH2 domain
Structure domains: SH2 domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry, simulated annealing
Expression system: Escherichia coli

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Citations

1 review citation

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