2ar5

X-ray diffraction
1.8Å resolution

Crystal structure of the mammalian C2alpha-PI3 Kinase PX-domain

Released:
Source organism: Homo sapiens
Entry authors: Parkinson GN, Vines D, Driscoll PC, Djordjevic S

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 + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-126279 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 14.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O00443 (Residues: 1421-1534; Coverage: 7%)
Gene name: PIK3C2A
Sequence domains: PX domain
Structure domains: Phox-like domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P3121
Unit cell:
a: 56.554Å b: 56.554Å c: 92.894Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.223 0.222 0.244
Expression system: Escherichia coli