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:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero hexamer (preferred)
PDBe Complex ID:
PDB-CPX-229669 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ig-like domain-containing protein
Molecule details ›
Chains: B, L
Length: 218 amino acids
Theoretical weight: 23.96 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains: Immunoglobulins
Length: 218 amino acids
Theoretical weight: 23.96 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical:
A2NHM3 (Residues: 1-114, 115-217; Coverage: 99%)
Sequence domains:
Structure domains: Immunoglobulins
Matrix metalloproteinase-14
Molecule details ›
Chains: C, M
Length: 13 amino acids
Theoretical weight: 1.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
Length: 13 amino acids
Theoretical weight: 1.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
- Canonical: P50281 (Residues: 215-227; Coverage: 2%)
