CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.390 | Collagenase (Catalytic Domain) |
|
3.40.390.10 | Collagenase (Catalytic Domain) |
Domain Context
CATH Clusters
| Superfamily | Collagenase (Catalytic Domain) |
| Functional Family | Disintegrin and metalloproteinase domain-containing protein 22 |
Enzyme Information
| 3.4.24.42 |
Atrolysin C.
based on mapping to UniProt P15167
Cleavage of 5-His-|-Leu-6, 10-His-|-Leu-11, 14-Ala-|-Leu-15, 16-Tyr-|-Leu-17 and 23-Gly-|-Phe-24 of insulin B chain. With small molecule substrates prefers hydrophobic residue at P2' and small residue such as Ala, Gly at P1.
-!- Hemorrhagic endopeptidase from the venom of the western diamondback rattlesnake (Crotalus atrox). -!- Exist as two forms, c and d. -!- Digests type IV collagen. -!- Phosphoramidon inhibits in the 0.1 mM range. -!- Hemorrhagic toxin-2 of C.ruber ruber has the same molecular weight and specificity. -!- Belongs to peptidase family M12B.
|
UniProtKB Entries (1)
| P15167 |
VM1AD_CROAT
Crotalus atrox
Snake venom metalloproteinase atrolysin-D
|
PDB Structure
| PDB | 1DTH |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Batimastat, a potent matrix mealloproteinase inhibitor, exhibits an unexpected mode of binding.
Proc.Natl.Acad.Sci.USA
|
