6e7f

X-ray diffraction
2.5Å resolution

Crystal Structure of Human Inositol Polyphosphate Multikinase (IPMK) Catalytic Core Domain

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)
PDBe Complex ID:
PDB-CPX-185540 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol polyphosphate multikinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 278 amino acids
Theoretical weight: 31.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q8NFU5 (Residues: 70-279, 374-416; 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 21-ID-F
Spacegroup: P21212
Unit cell:
a: 95.66Å b: 109.36Å c: 73.6Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.229 0.226 0.28
Expression system: Escherichia coli BL21(DE3)