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 | Peptidyl-prolyl cis-trans isomerase FKBP1A |
Enzyme Information
| 5.2.1.8 |
Peptidylprolyl isomerase.
based on mapping to UniProt P62942
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)
| P42345 |
MTOR_HUMAN
Homo sapiens
Serine/threonine-protein kinase mTOR
|
PDB Structure
| PDB | 1FAP |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP.
Science
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