X-ray diffraction
3.15Å resolution

Crystal structure of PTEN with a tetra-phosphorylated tail (4p-crPTEN-13sp-T2, SDTTDSDPENEG)

Source organism: Homo sapiens
Entry authors: Dempsey D, Phan K, Cole P, Gabelli SB

Function and Biology Details

Reactions catalysed:
[a protein]-serine/threonine phosphate + H(2)O = [a protein]-serine/threonine + phosphate
Phosphatidylinositol 3,4,5-trisphosphate + H(2)O = phosphatidylinositol 4,5-bisphosphate + phosphate
Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN Chain: A
Molecule details ›
Chain: A
Length: 349 amino acids
Theoretical weight: 40.89 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
  • Canonical: P60484 (Residues: 7-353, 378-390; Coverage: 83%)
  • Best match: P60484-3 (Residues: 7-55, 56-149)
Gene names: MMAC1, PTEN, TEP1
Sequence domains: C2 domain of PTEN tumour-suppressor protein

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: OTHER
Spacegroup: I4
Unit cell:
a: 113.444Å b: 113.444Å c: 57.005Å
α: 90° β: 90° γ: 90°
R R work R free
0.189 0.184 0.289
Expression system: Trichoplusia ni