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 |
Enzyme Information
| 5.2.1.8 |
Peptidylprolyl isomerase.
based on mapping to UniProt Q15257
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)
| Q15257 |
PTPA_HUMAN
Homo sapiens
Serine/threonine-protein phosphatase 2A activator
|
PDB Structure
| PDB | 4NY3 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural basis for PTPA interaction with the invariant C-terminal tail of PP2A.
Biol.Chem.
|