› 4hne

X-ray diffraction
2.95Å resolution

Crystal structure of the catalytic domain of human type II alpha Phosphatidylinositol 4-kinase (PI4KIIalpha) in complex with ADP

Released:
DOI: 10.2210/pdb4hne/pdb
PDB entry 4hne coloured by chain, front view.
PDB entry 4hne coloured by chain, side view.
PDB entry 4hne coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Molecular insights into the membrane-associated phosphatidylinositol 4-kinase IIα.
Zhou Q, Li J, Yu H, Zhai Y, Gao Z, Liu Y, Pang X, Zhang L, Schulten K, Sun F, Chen C
Nat Commun 5 3552 (2014)
PMID: 24675427

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo hexadecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189725 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylinositol 4-kinase type 2-alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 384 amino acids
Theoretical weight: 43.82 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9BTU6 (Residues: 78-453; Coverage: 79%)
Gene name: PI4K2A
Sequence domains: Phosphatidylinositol 3- and 4-kinase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: I422
Unit cell:
a: 191.824Å b: 191.824Å c: 157.543Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.251
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.
Muller et al. (2019)
7 more

35 mentions without citation

Biologically relevant oxidants and terminology, classification and nomenclature of oxidatively generated damage to nucleobases and 2-deoxyribose in nucleic acids.
Cadet et al. (2012)
34 more