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 16 (Predicted) |
Enzyme Information
| 3.1.3.16 |
Protein-serine/threonine phosphatase.
based on mapping to UniProt Q9BY84
[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).
|
| 3.1.3.48 |
Protein-tyrosine-phosphatase.
based on mapping to UniProt Q9BY84
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)
| Q9BY84 |
DUS16_HUMAN
Homo sapiens
Dual specificity protein phosphatase 16
|
PDB Structure
| PDB | 3TG3 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
A Distinct Interaction Mode Revealed by the Crystal Structure of the Kinase p38alpha with the MAPK Binding Domain of the Phosphatase MKP5.
Sci.Signal.
|
