› 5okp

X-ray diffraction
1.85Å resolution

Crystal structure of human SHIP2 Phosphatase-C2 double mutant F593D/L597D

Released:
DOI: 10.2210/pdb5okp/pdb
PDB entry 5okp coloured by chain, front view.
PDB entry 5okp coloured by chain, side view.
PDB entry 5okp 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 Chain: A
Molecule details ›
Chain: A
Length: 461 amino acids
Theoretical weight: 52.72 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15357 (Residues: 420-878; Coverage: 37%)
Gene names: INPPL1, SHIP2

Ligands and Environments

1 bound ligand:
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Unit cell:
a: 43.745Å b: 73.426Å c: 157.964Å
α: 90° β: 90.7° γ: 90°
R-values:
R R work R free
0.179 0.178 0.205
Expression system: Escherichia coli BL21(DE3)

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Citations

4 review citations

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