› 5okm

X-ray diffraction
1.96Å resolution

Crystal structure of human SHIP2 Phosphatase-C2

Released:
DOI: 10.2210/pdb5okm/pdb
PDB entry 5okm coloured by chain, front view.
PDB entry 5okm coloured by chain, side view.
PDB entry 5okm coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for interdomain communication in SHIP2 providing high phosphatase activity.
Le Coq J, Camacho-Artacho M, Velázquez JV, Santiveri CM, Gallego LH, Campos-Olivas R, Dölker N, Lietha D
Elife 6 (2017)
PMID: 28792888

Function and Biology Details

Reaction catalysed: 
1-phosphatidyl-1D-myo-inositol 3,4,5-triphosphate + H(2)O = 1-phosphatidyl-1D-myo-inositol 3,4-diphosphate + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127447 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase 2 Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 461 amino acids
Theoretical weight: 52.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O15357 (Residues: 420-878; Coverage: 37%)
Gene names: INPPL1, SHIP2

Ligands and Environments

3 bound ligands:
Ligand B3P 7 x B3P
Ligand NO3 2 x NO3
Ligand EDO 21 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P212121
Unit cell:
a: 136.037Å b: 175.836Å c: 176.893Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.18 0.208
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The impact of phosphoinositide 5-phosphatases on phosphoinositides in cell function and human disease.
Ramos et al. (2019)
2 more

5 mentions without citation

Targeting SHIP1 and SHIP2 in Cancer.
Pedicone et al. (2021)
4 more