› 6srr

X-ray diffraction
2.45Å resolution

Crystal structure of human SHIP2 catalytic domain

Released:
DOI: 10.2210/pdb6srr/pdb
PDB entry 6srr coloured by chain, front view.
PDB entry 6srr coloured by chain, side view.
PDB entry 6srr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Allosteric Site on SHIP2 Identified Through Fluorescent Ligand Screening and Crystallography: A Potential New Target for Intervention.
Whitfield H, Hemmings AM, Mills SJ, Baker K, White G, Rushworth S, Riley AM, Potter BVL, Brearley CA
J Med Chem 64 3813-3826 (2021)
PMID: 33724834

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
UniProt:
  • Canonical: O15357 (Residues: 419-732; Coverage: 25%)
Gene names: INPPL1, SHIP2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 45.13Å b: 62.12Å c: 115.62Å
α: 90° β: 92.38° γ: 90°
R-values:
R R work R free
0.189 0.186 0.237
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Crystal Structure and Enzymology of Solanum tuberosum Inositol Tris/Tetrakisphosphate Kinase 1 (StITPK1).
Whitfield et al. (2024)

1 mention without citation

Allosteric Site on SHIP2 Identified Through Fluorescent Ligand Screening and Crystallography: A Potential New Target for Intervention.
Whitfield et al. (2021)