Function and Biology Details
Reaction catalysed:
Preferential cleavage where P1', P2' and P3' are hydrophobic residues.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Stromelysin-1 and Metalloproteinase inhibitor 1 (preferred)
PDBe Complex ID:
PDB-CPX-133885 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Stromelysin-1
Molecule details ›
Chains: A, C
Length: 173 amino acids
Theoretical weight: 19.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Length: 173 amino acids
Theoretical weight: 19.51 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
P08254 (Residues: 100-272; Coverage: 38%)
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Metalloproteinase inhibitor 1
Molecule details ›
Chains: B, D
Length: 184 amino acids
Theoretical weight: 20.65 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains:
Length: 184 amino acids
Theoretical weight: 20.65 KDa
Source organism: Homo sapiens
Expression system: Cricetulus griseus
UniProt:
- Canonical: P01033 (Residues: 24-207; Coverage: 100%)
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains:
