Function and Biology Details
Reaction catalysed:
Cleavage of interstitial collagens in the triple helical domain. Unlike EC 3.4.24.7, this enzyme cleaves type III collagen more slowly than type I.
Biochemical function:
Biological process:
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Neutrophil collagenase and peptide (preferred)
PDBe Complex ID:
PDB-CPX-149835 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Neutrophil collagenase
Molecule details ›
Chains: A, F
Length: 158 amino acids
Theoretical weight: 17.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Length: 158 amino acids
Theoretical weight: 17.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P22894 (Residues: 105-262; Coverage: 35%)
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
