6m89

X-ray diffraction
1.85Å resolution

Crystal structure of the core catalytic domain of human inositol phosphate multikinase in complex with quercetin

Released:

Function and Biology Details

Reactions catalysed:
ATP + 1D-myo-inositol 1,3,4,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate
(1a) ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate
ATP + 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol polyphosphate multikinase Chain: A
Molecule details ›
Chain: A
Length: 261 amino acids
Theoretical weight: 29.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8NFU5 (Residues: 50-262, 378-416; Coverage: 61%)
Gene names: IMPK, IPMK
Sequence domains: Inositol polyphosphate kinase

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P42212
Unit cell:
a: 77.956Å b: 77.956Å c: 84.468Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.174 0.234
Expression system: Escherichia coli