CATH Domain 4jmkA00

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	Dual specificity protein phosphatase 8

Enzyme Information

3.1.3.48

Protein-tyrosine-phosphatase.

based on mapping to UniProt Q13202

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.

3.1.3.16

Protein-serine/threonine phosphatase.

based on mapping to UniProt Q13202

[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).

UniProtKB Entries (1)

Q13202

DUS8_HUMAN

Homo sapiens

Dual specificity protein phosphatase 8

PDB Structure

PDB	4JMK
External Links	PDBSum Proteopedia
Method	X-RAY DIFFRACTION
Organism
Primary Citation	The family-wide structure and function of human dual-specificity protein phosphatases. Jeong, D.G., Wei, C.H., Ku, B., Jeon, T.J., Chien, P.N., Kim, J.K., Park, S.Y., Hwang, H.S., Ryu, S.Y., Park, H., Kim, D.S., Kim, S.J., Ryu, S.E. Acta Crystallogr.,Sect.D