PDBe 5bzx

X-ray diffraction
2.5Å resolution

Crystal structure of human phosphatase PTEN treated with a bisperoxovanadium complex

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
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
Macromolecule:
Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 314 amino acids
Theoretical weight: 37.31 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P60484 (Residues: 14-351; Coverage: 78%)
Gene names: MMAC1, PTEN, TEP1
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: C2221
Unit cell:
a: 207.06Å b: 206.9Å c: 87.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.177 0.175 0.204
Expression system: Trichoplusia ni