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:
- not assigned
Cellular component:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Matrix metalloproteinase-14 and Radixin (preferred)
PDBe Complex ID:
PDB-CPX-150650 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Radixin
Molecule details ›
Chain: A
Length: 312 amino acids
Theoretical weight: 36.92 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 312 amino acids
Theoretical weight: 36.92 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
- Canonical:
P26043 (Residues: 1-310; Coverage: 53%)
Sequence domains:
Structure domains:
Matrix metalloproteinase-14
Molecule details ›
Chain: B
Length: 20 amino acids
Theoretical weight: 2.47 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
Length: 20 amino acids
Theoretical weight: 2.47 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
- Canonical: P50281 (Residues: 563-582; Coverage: 4%)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SPRING-8 BEAMLINE BL38B1
Spacegroup:
P6122
Expression systems:
- Escherichia coli
- Not provided
