Function and Biology Details
Reaction catalysed:
Similar to stromelysin 1, but action on collagen types III, IV and V is weak.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Peptidase M10A
- Tissue inhibitor of metalloproteinases-like, OB-fold
- Protease inhibitor I35 (TIMP)
- Peptidase M10A, catalytic domain
- Peptidase M10, metallopeptidase
- Peptidase, metallopeptidase
- Metallopeptidase, catalytic domain superfamily
- Tissue inhibitor of metalloproteinase, conserved site
2 more domains
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Stromelysin-2 and Metalloproteinase inhibitor 1 (preferred)
PDBe Complex ID:
PDB-CPX-133886 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Metalloproteinase inhibitor 1
Molecule details ›
Chain: A
Length: 184 amino acids
Theoretical weight: 20.69 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains:
Length: 184 amino acids
Theoretical weight: 20.69 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
- Canonical:
P01033 (Residues: 24-207; Coverage: 100%)
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains:
Stromelysin-2
Molecule details ›
Chain: B
Length: 165 amino acids
Theoretical weight: 18.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Length: 165 amino acids
Theoretical weight: 18.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P09238 (Residues: 99-263; Coverage: 36%)
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
