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 P0ABZ6
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 (2)
| P0ABZ6 |
SURA_ECOLI
Escherichia coli K-12
Chaperone SurA
|
| Q2RHX9 |
Q2RHX9_MOOTA
Moorella thermoacetica ATCC 39073
Glycosyl transferase, group 1
|
PDB Structure
| PDB | 2PV1 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues.
J.Mol.Biol.
|
