CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.40 | 3-Layer(aba) Sandwich | |
3.40.250 | Oxidized Rhodanese; domain 1 | |
3.40.250.10 | Rhodanese-like domain |
Domain Context
CATH Clusters
Superfamily | Rhodanese-like domain |
Functional Family | Dual specificity phosphatase 7 |
Enzyme Information
3.1.3.48 |
Protein-tyrosine-phosphatase.
based on mapping to UniProt Q16828
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 Q16828
[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)
Q16828 |
DUS6_HUMAN
Homo sapiens
Dual specificity protein phosphatase 6
|
PDB Structure
PDB | 1HZM |
External Links | |
Method | SOLUTION NMR |
Organism | Escherichia |
Primary Citation |
Solution structure of ERK2 binding domain of MAPK phosphatase MKP-3: structural insights into MKP-3 activation by ERK2.
Mol.Cell
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