2a98

X-ray diffraction
2.6Å resolution

Crystal structure of the catalytic domain of human inositol 1,4,5-trisphosphate 3-kinase C

Released:
Source organism: Homo sapiens
Entry authors: Hallberg BM, Ogg D, Ehn M, Graslund S, Hammarstrom M, Kotenyova T, Nilsson-Ehle P, Nordlund P, Persson C, Sagemark J, Schuler H, Stenmark P, Thorsell A-G, Arrowsmith C, Edwards A, Sundstrom M, Weigelt J, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,3,4,5-tetrakisphosphate
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188444 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inositol-trisphosphate 3-kinase C Chain: A
Molecule details ›
Chain: A
Length: 259 amino acids
Theoretical weight: 29.64 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96DU7 (Residues: 425-683; Coverage: 38%)
Gene names: IP3KC, ITPKC
Sequence domains: Inositol polyphosphate kinase
Structure domains: Inositol polyphosphate kinase

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P6122
Unit cell:
a: 87.72Å b: 87.72Å c: 174.94Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.22 0.218 0.262
Expression system: Escherichia coli