CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.60 | 4-Layer Sandwich | |
3.60.21 | Purple Acid Phosphatase; chain A, domain 2 | |
3.60.21.10 | Metallo-dependent phosphatases |
Domain Context
CATH Clusters
Superfamily | 3.60.21.10 |
Functional Family | Serine/threonine-protein phosphatase |
Enzyme Information
3.1.3.16 |
Protein-serine/threonine phosphatase.
based on mapping to UniProt P62136
[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).
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UniProtKB Entries (2)
O55000 |
PP1RA_RAT
Rattus norvegicus
Serine/threonine-protein phosphatase 1 regulatory subunit 10
|
P62136 |
PP1A_HUMAN
Homo sapiens
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
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PDB Structure
PDB | 4MP0 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code.
Proc.Natl.Acad.Sci.USA
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