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 3 |
Enzyme Information
| 3.4.24.7 |
Interstitial collagenase.
based on mapping to UniProt P21692
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.
-!- The enzyme takes its name from substrates of the interstitial collagen group - types I, II and III, all of which are cleaved in the helical domain. -!- Alpha-macroglobulins are cleaved much more rapidly. -!- The enzyme is widely distributed in vertebrate animals. -!- Belongs to peptidase family M10B.
|
UniProtKB Entries (1)
| P21692 |
MMP1_PIG
Sus scrofa
Interstitial collagenase
|
PDB Structure
| PDB | 1FBL |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structure of full-length porcine synovial collagenase reveals a C-terminal domain containing a calcium-linked, four-bladed beta-propeller.
Structure
|
