PDBe 2rea

X-ray diffraction
2.5Å resolution

Crystal structures of C2ALPHA-PI3 kinase PX-domain domain indicate conformational change associated with ligand binding.

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (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: 1421-1532; Coverage: 7%)
Gene name: PIK3C2A
Structure domains: Phox-like domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P3121
Unit cell:
a: 56.866Å b: 56.866Å c: 92.995Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.235 0.231 0.318
Expression system: Escherichia coli