CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.10 | Roll |
|
3.10.50 | Chitinase A; domain 3 |
|
3.10.50.40 |
Domain Context
CATH Clusters
| Superfamily | 3.10.50.40 |
| Functional Family | Peptidylprolyl isomerase |
Enzyme Information
| 5.2.1.8 |
Peptidylprolyl isomerase.
based on mapping to UniProt Q9SCY2
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)
| Q9SCY2 |
FKB13_ARATH
Arabidopsis thaliana
Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic
|
PDB Structure
| PDB | 1U79 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen
Proc.Natl.Acad.Sci.Usa
|