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
| 3.4.21.106 |
Hepsin.
based on mapping to UniProt P05981
Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys.
-!- This type-II membrane-associated serine peptidase has been implicated in cell growth and development. -!- The enzyme has been shown to activate blood coagulation factor VII by cleavage of the 152-Arg-|-Ile-153 peptide bound in BHK cells, thus indicating a possible role in the initiation of blood coagulation. -!- There is no cleavage after aromatic or aliphatic residues. -!- The occupancy of the S2 site is an absolute requirement for catalysis and a basic residue at that site is preferred to an aliphatic residue. -!- The nature of the residue at S3 also affects hydrolysis, with Gln being much more favorable than Ala. -!- Belongs to peptidase family S1A.
|
UniProtKB Entries (1)
| P05981 |
HEPS_HUMAN
Homo sapiens
Serine protease hepsin
|
PDB Structure
| PDB | 5CE1 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal Structure of Serine protease Hepsin in complex with Inhibitor
To Be Published
|
