CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.287 | Helix Hairpins |
|
1.10.287.460 | Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Peptidyl-prolyl cis-trans isomerase, FKBP-type, N-terminal domain |
| Functional Family | Peptidyl-prolyl cis-trans isomerase |
Enzyme Information
| 5.2.1.8 |
Peptidylprolyl isomerase.
based on mapping to UniProt P45523
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)
| P45523 |
FKBA_ECOLI
Escherichia coli K-12
FKBP-type peptidyl-prolyl cis-trans isomerase FkpA
|
PDB Structure
| PDB | 1Q6U |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity.
J.Mol.Biol.
|
