CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.40 | Beta Barrel |
|
2.40.10 | Thrombin, subunit H |
|
2.40.10.10 | Trypsin-like serine proteases |
Domain Context
CATH Clusters
| Superfamily | Trypsin-like serine proteases |
| Functional Family |
Enzyme Information
| 3.4.21.12 |
Alpha-lytic endopeptidase.
based on mapping to UniProt P00778
Preferential cleavage: Ala-|-Xaa, Val-|-Xaa in bacterial cell walls, elastin and other proteins.
-!- Belongs to peptidase family S1E.
|
UniProtKB Entries (1)
| P00778 |
PRLA_LYSEN
Lysobacter enzymogenes
Alpha-lytic protease
|
PDB Structure
| PDB | 2H5C |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Subangstrom crystallography reveals that short ionic hydrogen bonds, and not a His-Asp low-barrier hydrogen bond, stabilize the transition state in serine protease catalysis
J.Am.Chem.Soc.
|
