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
| 3.4.21.32 |
Brachyurin.
based on mapping to UniProt P00771
Hydrolysis of proteins, with broad specificity for peptide bonds. Native collagen is cleaved about 75% of the length of the molecule from the N-terminus. Low activity on small molecule substrates of both trypsin and chymotrypsin.
-!- From hepatopancreas of the fiddler crab (Uca pugilator). -!- Other serine endopeptidases that degrade collagen, but are not listed separately here, include a second endopeptidase from U.pugilator, digestive enzymes from other decapod crustacea, and an enzyme from the fungus Entomophthora coronata. -!- Belongs to peptidase family S1.
|
UniProtKB Entries (2)
| P23827 |
ECOT_ECOLI
Escherichia coli K-12
Ecotin
|
| P00771 |
COGS_LEPPG
Leptuca pugilator
Brachyurin
|
PDB Structure
| PDB | 1AZZ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Crystal structure of an ecotin-collagenase complex suggests a model for recognition and cleavage of the collagen triple helix.
Biochemistry
|
