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 |
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 (3)
| P0A7V3 |
RS3_ECOLI
Escherichia coli K-12
30S ribosomal protein S3
|
| P62942 |
FKB1A_HUMAN
Homo sapiens
Peptidyl-prolyl cis-trans isomerase FKBP1A
|
| Q5SLE7 |
Q5SLE7_THET8
Thermus thermophilus HB8
Peptidyl-prolyl cis-trans isomerase
|
PDB Structure
| PDB | 4ODQ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Molecular insights into substrate recognition and catalytic mechanism of the chaperone and FKBP peptidyl-prolyl isomerase SlyD.
BMC Biol.
|