3t54

X-ray diffraction
1.9Å resolution

Crystal structure of the catalytic domain of human diphosphoinositol pentakisphosphate kinase 2 (PPIP5K2) in complex with ATP and Cadmium

Released:
Source organism: Homo sapiens

Function and Biology Details

Reactions catalysed:
ATP + 1D-myo-inositol 1-diphosphate 2,3,4,5,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
ATP + 1D-myo-inositol 5-diphosphate 1,2,3,4,6-pentakisphosphate = ADP + 1D-myo-inositol 1,5-bis(diphosphate) 2,3,4,6-tetrakisphosphate
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol hexakisphosphate and diphosphoinositol-pentakisphosphate kinase 2 Chain: A
Molecule details ›
Chain: A
Length: 334 amino acids
Theoretical weight: 37.97 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O43314 (Residues: 37-366; Coverage: 27%)
Gene names: HISPPD1, KIAA0433, PPIP5K2, VIP2
Sequence domains: Diphosphoinositol pentakisphosphate kinase 2 N-terminal domain
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: P212121
Unit cell:
a: 89.957Å b: 110.597Å c: 41.307Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.2 0.198 0.226
Expression system: Escherichia coli