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 Q9LDC0
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)
| Q9LDC0 |
FKB42_ARATH
Arabidopsis thaliana
Peptidyl-prolyl cis-trans isomerase FKBP42
|
PDB Structure
| PDB | 2IF4 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal Structure of a Multi-domain Immunophilin from Arabidopsis thaliana: A Paradigm for Regulation of Plant ABC Transporters.
J.Mol.Biol.
|
