CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.25 | Alpha Horseshoe |
|
1.25.40 | Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat |
|
1.25.40.10 | Tetratricopeptide repeat domain |
Domain Context
CATH Clusters
| Superfamily | Tetratricopeptide repeat domain |
| Functional Family | Peptidylprolyl isomerase |
Enzyme Information
| 5.2.1.8 |
Peptidylprolyl isomerase.
based on mapping to UniProt Q13451
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)
| Q13451 |
FKBP5_HUMAN
Homo sapiens
Peptidyl-prolyl cis-trans isomerase FKBP5
|
PDB Structure
| PDB | 1KT0 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of the large FK506-binding protein FKBP51, an Hsp90-binding protein and a
component of steroid receptor complexes
Proc.Natl.Acad.Sci.USA
|
