› 6ux9

X-ray diffraction
1.71Å resolution

Function and Biology Details

Reaction catalysed: 
ATP + 1-phosphatidyl-1D-myo-inositol 5-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155728 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 370 amino acids
Theoretical weight: 42.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48426 (Residues: 35-405; Coverage: 86%)
Gene names: PI5P4KA, PIP4K2A, PIP5K2, PIP5K2A
Sequence domains: Phosphatidylinositol-4-phosphate 5-Kinase

Ligands and Environments

1 bound ligand:
Ligand UHJ 2 x UHJ
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 44.23Å b: 88.58Å c: 105.78Å
α: 90° β: 92.91° γ: 90°
R-values:
R R work R free
0.178 0.177 0.204
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Expanding role of PI5P4Ks in cancer: A promising druggable target.
Arora et al. (2022)
2 more

3 mentions without citation

Advances in chemical proteomic evaluation of lipid kinases-DAG kinases as a case study.
Ware et al. (2021)
2 more