9b4s

X-ray diffraction
3.1Å resolution

Crystal structure of the RRAS2-p110alpha complex

Released:
Model geometry
Fit model/data

Function and Biology Details

Reactions catalysed:
ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-284253 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform Chain: A
Molecule details ›
Chain: A
Length: 965 amino acids
Theoretical weight: 112.03 KDa
Source organism: Homo sapiens
Expression system: Trichoplacea
UniProt:
  • Canonical: P42336 (Residues: 105-1068; Coverage: 90%)
Gene name: PIK3CA
Sequence domains:
Ras-related protein R-Ras2 Chain: B
Molecule details ›
Chain: B
Length: 180 amino acids
Theoretical weight: 20.56 KDa
Source organism: Homo sapiens
Expression system: Trichoplacea
UniProt:
  • Canonical: P62070 (Residues: 1-179; Coverage: 88%)
  • Best match: P62070-2 (Residues: 1-102)
Gene names: RRAS2, TC21
Sequence domains: Ras family

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P42212
Unit cell:
a: 181.488Å b: 181.488Å c: 96.03Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.23 0.272
Expression system: Trichoplacea