CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
2 | Mainly Beta |
|
2.110 | 4 Propeller |
|
2.110.10 | Hemopexin |
|
2.110.10.10 | Hemopexin-like domain |
Domain Context
CATH Clusters
| Superfamily | Hemopexin-like domain |
| Functional Family | Matrix metallopeptidase 24 |
Enzyme Information
| 3.4.24.80 |
Membrane-type matrix metalloproteinase-1.
based on mapping to UniProt P50281
Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe- 342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.
-!- Believed to play an important role in the activation of progelatinase A at cell surfaces. -!- Belongs to peptidase family M10.
|
UniProtKB Entries (1)
| P02647 |
APOA1_HUMAN
Homo sapiens
Apolipoprotein A-I
|
PDB Structure
| PDB | 6CLZ |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
MT1-MMP Binds Membranes by Opposite Tips of Its beta Propeller to Position It for Pericellular Proteolysis.
Structure
|
