CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.128 | Lipocalin |
|
2.40.128.90 | OMPT-like |
Domain Context
CATH Clusters
| Superfamily | OMPT-like |
| Functional Family |
Enzyme Information
| 3.4.23.49 |
Omptin.
based on mapping to UniProt P09169
Has a virtual requirement for Arg in the P1 position and a slightly less stringent preference for this residue in the P1' position, which can also contain Lys, Gly or Val.
-!- Shows a preference for cleavage between consecutive basic amino acids, but is capable of cleavage when P1' is a non-basic residue. -!- Belongs to peptidase family A26. -!- Formerly EC 3.4.21.87.
|
UniProtKB Entries (1)
| P09169 |
OMPT_ECOLI
Escherichia coli K-12
Protease 7
|
PDB Structure
| PDB | 1I78 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of the outer membrane protease OmpT from Escherichia coli suggests a novel catalytic site.
EMBO J.
|