7jtx

X-ray diffraction
3.23Å resolution

the structural basis of PTEN regulation by multi-site phosphorylation

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
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-158017 (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: 366 amino acids
Theoretical weight: 42.34 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P60484 (Residues: 7-362, 363-395; Coverage: 90%)
Gene names: MMAC1, PTEN, TEP1
Sequence domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: I4
Unit cell:
a: 111.865Å b: 111.865Å c: 60.656Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.228 0.263
Expression system: Spodoptera frugiperda