Function and Biology Details
Reaction catalysed:
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.
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
22 kDa interstitial collagenase (preferred)
PDBe Complex ID:
PDB-CPX-137297 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
22 kDa interstitial collagenase
Molecule details ›
Chains: A, G, M
Length: 156 amino acids
Theoretical weight: 17.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Length: 156 amino acids
Theoretical weight: 17.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P03956 (Residues: 106-261; Coverage: 35%)
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
