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 | serine protease hepsin |
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 | 1O5F |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Pichia |
Primary Citation |
Dissecting and designing inhibitor selectivity determinants at the S1 site using an artificial Ala190 protease (Ala190 uPA).
J.Mol.Biol.
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