› 7n7j

X-ray diffraction
2.1Å resolution

Crystal Structure of PI5P4KIIAlpha complex with AMPPNP

Released:
DOI: 10.2210/pdb7n7j/pdb
Model geometry
Fit model/data
PDB entry 7n7j coloured by chain, front view.
PDB entry 7n7j coloured by chain, side view.
PDB entry 7n7j coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Pharmacological inhibition of PI5P4Kα/β disrupts cell energy metabolism and selectively kills p53-null tumor cells.
Chen S, Chandra Tjin C, Gao X, Xue Y, Jiao H, Zhang R, Wu M, He Z, Ellman J, Ha Y
Proc Natl Acad Sci U S A 118 (2021)
PMID: 34001596

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:
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 Chain: A
Molecule details ›
Chain: A
Length: 377 amino acids
Theoretical weight: 43.11 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P48426 (Residues: 33-405; Coverage: 92%)
  • Best match: P48426-2 (Residues: 1-346)
Gene names: PI5P4KA, PIP4K2A, PIP5K2, PIP5K2A
Sequence domains: Phosphatidylinositol-4-phosphate 5-Kinase

Ligands and Environments

3 bound ligands:
Ligand MN 2 x MN
Ligand ANP 1 x ANP
Ligand SO4 3 x SO4
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P6122
Unit cell:
a: 136.074Å b: 136.074Å c: 95.141Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.215 0.213 0.251
Expression system: Escherichia coli

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Citations

6 review citations

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