CATH Classification

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 P03956
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)

P03956
MMP1_HUMAN
Homo sapiens
Interstitial collagenase

PDB Structure

PDB 1SU3
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
X-ray structure of human proMMP-1: new insights into procollagenase activation and collagen binding.
Jozic, D., Bourenkov, G., Lim, N.H., Visse, R., Nagase, H., Bode, W., Maskos, K.
J.Biol.Chem.