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X-ray diffraction
2Å resolution

Crystal structure of Inositol Phosphate Multikinase Ipk2 from S. cerevisiae

Released:
DOI: 10.2210/pdb2iew/pdb
Model geometry
Fit model/data
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Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of inositol phosphate multikinase 2 and implications for substrate specificity.
Holmes W, Jogl G
J Biol Chem 281 38109-16 (2006)
PMID: 17050532

Function and Biology Details

Reactions catalysed: 
1D-myo-inositol 1,4,5-trisphosphate + ATP = 1D-myo-inositol 1,3,4,5-tetrakisphosphate + ADP + H(+).
1D-myo-inositol 1,4,5-trisphosphate + 2 ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + 2 ADP + 2 H(+).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139455 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol polyphosphate multikinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 363 amino acids
Theoretical weight: 41.47 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P07250 (Residues: 1-355; Coverage: 100%)
Gene names: ARG82, ARGR3, GSL3, IPK2, YD9395.06C, YDR173C
Sequence domains: Inositol polyphosphate kinase
Structure domains: Inositol polyphosphate kinase

Ligands and Environments

1 bound ligand:
Ligand CA 1 x CA
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: NSLS BEAMLINE X4A
Spacegroup: P63
Unit cell:
a: 186.51Å b: 186.51Å c: 50.12Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.211 0.208 0.253
Expression system: Escherichia coli

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Citations

10 review citations

Inositol polyphosphates: a new frontier for regulating gene expression.
Alcázar-Román et al. (2008)
9 more

6 mentions without citation

The enzymes of human diphosphoinositol polyphosphate metabolism.
Thomas et al. (2014)
5 more