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:
Metalloproteinase inhibitor 2 and Stromelysin-2 (preferred)
PDBe Complex ID:
PDB-CPX-140607 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Metalloproteinase inhibitor 2
Molecule details ›
Chains: A, B
Length: 194 amino acids
Theoretical weight: 21.78 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains:
Length: 194 amino acids
Theoretical weight: 21.78 KDa
Source organism: Homo sapiens
Expression system: Homo sapiens
UniProt:
- Canonical:
P16035 (Residues: 27-220; Coverage: 100%)
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains:
Stromelysin-2
Molecule details ›
Chains: D, F
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)
