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 Pin1 |
Enzyme Information
| 5.2.1.8 |
Peptidylprolyl isomerase.
based on mapping to UniProt Q13526
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)
| Q13526 |
PIN1_HUMAN
Homo sapiens
Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1
|
PDB Structure
| PDB | 2RUD |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
The C113D mutation in human Pin1 causes allosteric structural changes in the phosphate binding pocket of the PPIase domain through the tug of war in the dual-histidine motif.
Biochemistry
|