CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.10 | Thrombin, subunit H |
|
2.40.10.330 |
Domain Context
CATH Clusters
| Superfamily | 2.40.10.330 |
| Functional Family | Peptidyl-prolyl cis-trans isomerase |
Enzyme Information
| 5.2.1.8 |
Peptidylprolyl isomerase.
based on mapping to UniProt P0A9K9
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)
| P0A9K9 |
SLYD_ECOLI
Escherichia coli K-12
FKBP-type peptidyl-prolyl cis-trans isomerase SlyD
|
PDB Structure
| PDB | 2KFW |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
The interaction of the Escherichia coli protein SlyD with nickel ions illuminates the mechanism of regulation of its peptidyl-prolyl isomerase activity.
Febs J.
|