Function and Biology Details
Reaction catalysed:
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.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-538278 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Matrix metalloproteinase-14
Molecule details ›
Chain: M
Length: 174 amino acids
Theoretical weight: 19.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Length: 174 amino acids
Theoretical weight: 19.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P50281 (Residues: 114-287; Coverage: 31%)
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Metalloproteinase inhibitor 2
Molecule details ›
Chain: T
Length: 184 amino acids
Theoretical weight: 20.53 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains:
Length: 184 amino acids
Theoretical weight: 20.53 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
- Canonical: P16368 (Residues: 27-210; Coverage: 95%)
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains:
