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:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133887 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Matrix metalloproteinase-14
Molecule details ›
Chains: A, D
Length: 181 amino acids
Theoretical weight: 20.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Length: 181 amino acids
Theoretical weight: 20.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P50281 (Residues: 112-292; Coverage: 32%)
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Metalloproteinase inhibitor 1
Molecule details ›
Chains: B, C
Length: 125 amino acids
Theoretical weight: 14.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 125 amino acids
Theoretical weight: 14.13 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical: P01033 (Residues: 24-148; Coverage: 68%)
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
