CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.120 | Four Helix Bundle (Hemerythrin (Met), subunit A) |
|
1.20.120.1150 | Phosphotyrosyl phosphate activator, C-terminal lid domain |
Domain Context
CATH Clusters
| Superfamily | 1.20.120.1150 |
| Functional Family | Serine/threonine-protein phosphatase 2A activator 1 |
Enzyme Information
| 5.2.1.8 |
Peptidylprolyl isomerase.
based on mapping to UniProt P40454
Peptidylproline (omega=180) = peptidylproline (omega=0).
-!- The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A. -!- Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli. -!- The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
|
UniProtKB Entries (1)
| P40454 |
PTPA1_YEAST
Saccharomyces cerevisiae S288C
Serine/threonine-protein phosphatase 2A activator 1
|
PDB Structure
| PDB | 2IXP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of the PP2A phosphatase activator: implications for its PP2A-specific PPIase activity.
Mol. Cell
|
