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 | Matrix metalloproteinase-14 preproprotein |
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)
| P50281 |
MMP14_HUMAN
Homo sapiens
Matrix metalloproteinase-14
|
PDB Structure
| PDB | 3MA2 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Intrinsic Protein Flexibility of Endogenous Protease Inhibitor TIMP-1 Controls Its Binding Interface and Affects Its Function.
Biochemistry
|