CATH Domain 1d5rA01

CATH Classification

Level	CATH Code	Description
	3	Alpha Beta
	3.90	Alpha-Beta Complex
	3.90.190	Protein-Tyrosine Phosphatase; Chain A
	3.90.190.10	Protein tyrosine phosphatase superfamily

Domain Context

CATH Clusters

Superfamily	Protein tyrosine phosphatase superfamily
Functional Family	Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

Enzyme Information

3.1.3.16	Protein-serine/threonine phosphatase. based on mapping to UniProt P60484 [a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate. -!- A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48). -!- The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
3.1.3.67	Phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase. based on mapping to UniProt P60484 Phosphatidylinositol 3,4,5-trisphosphate + H(2)O = phosphatidylinositol 4,5-bisphosphate + phosphate. -!- Does not dephosphorylate inositol 4,5-bisphosphate. -!- This enzyme still works when the 2,3-bis(acyloxy)propyl group is removed, i.e., it hydrolyzes Ins(1,3,4,5)P(4) to Ins(1,4,5)P(3).
3.1.3.48	Protein-tyrosine-phosphatase. based on mapping to UniProt P60484 Protein tyrosine phosphate + H(2)O = protein tyrosine + phosphate. -!- Dephosphorylates O-phosphotyrosine groups in phosphoproteins, such as the products of EC 2.7.10.2.

UniProtKB Entries (1)

PTEN_HUMAN

Homo sapiens

Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN

PDB Structure

PDB	1D5R
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism	Trichoplusia
Primary Citation	Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association. Lee, J.O., Yang, H., Georgescu, M.M., Di Cristofano, A., Maehama, T., Shi, Y., Dixon, J.E., Pandolfi, P., Pavletich, N.P. Cell(Cambridge,Mass.)