› 4a9c

X-ray diffraction
2.1Å resolution

Crystal structure of human SHIP2 in complex with biphenyl 2,3',4,5',6- pentakisphosphate

Released:
DOI: 10.2210/pdb4a9c/pdb
PDB entry 4a9c coloured by chain, front view.
PDB entry 4a9c coloured by chain, side view.
PDB entry 4a9c coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A synthetic polyphosphoinositide headgroup surrogate in complex with SHIP2 provides a rationale for drug discovery.
Mills SJ, Persson C, Cozier G, Thomas MP, Trésaugues L, Erneux C, Riley AM, Nordlund P, Potter BV
ACS Chem Biol 7 822-8 (2012)
PMID: 22330088

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
Molecule details ›
Chains: A, B
Length: 316 amino acids
Theoretical weight: 36.24 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15357 (Residues: 419-732; Coverage: 25%)
Gene names: INPPL1, SHIP2
Structure domains: Endonuclease/exonuclease/phosphatase

Ligands and Environments

1 bound ligand:
Ligand B5F 1 x B5F
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P21
Unit cell:
a: 45.246Å b: 61.52Å c: 114.742Å
α: 90° β: 91.94° γ: 90°
R-values:
R R work R free
0.202 0.201 0.221
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Inhibition of PI3K signaling spurs new therapeutic opportunities in inflammatory/autoimmune diseases and hematological malignancies.
Foster et al. (2012)
6 more

11 mentions without citation

Structural basis for interdomain communication in SHIP2 providing high phosphatase activity.
Le Coq et al. (2017)
10 more