PDBe 1d5r

X-ray diffraction
2.1Å resolution

Crystal Structure of the PTEN Tumor Suppressor

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN Chain: A
Molecule details ›
Chain: A
Length: 324 amino acids
Theoretical weight: 38.5 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P60484 (Residues: 7-353; Coverage: 80%)
Gene names: MMAC1, PTEN, TEP1
Sequence domains: Dual specificity phosphatase, catalytic domain
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE F2
Spacegroup: I4
Unit cell:
a: 113.14Å b: 113.14Å c: 58.55Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.226 0.224 0.276
Expression system: Trichoplusia ni