CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1000 | HAD superfamily/HAD-like |
Domain Context
CATH Clusters
| Superfamily | HAD superfamily/HAD-like |
| Functional Family | Carboxy-terminal domain RNA polymerase II polypeptide A small |
Enzyme Information
| 3.1.3.16 |
Protein-serine/threonine phosphatase.
based on mapping to UniProt Q9GZU7
[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)
| Q9GZU7 |
CTDS1_HUMAN
Homo sapiens
Carboxy-terminal domain RNA polymerase II polypeptide A small phosphatase 1
|
PDB Structure
| PDB | 6DU3 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Phosphatase activity of small C-terminal domain phosphatase 1 (SCP1) controls the stability of the key neuronal regulator RE1-silencing transcription factor (REST).
J. Biol. Chem.
|
