Function and Biology Details
Reaction catalysed:
Cleavage of gelatin type I and collagen types IV, V, VII, X. Cleaves the collagen-like sequence Pro-Gln-Gly-|-Ile-Ala-Gly-Gln.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
72 kDa type IV collagenase
Molecule details ›
Chains: A, B
Length: 631 amino acids
Theoretical weight: 71 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
Sequence domains:
Structure domains:
Length: 631 amino acids
Theoretical weight: 71 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
- Canonical:
P08253 (Residues: 30-660; Coverage: 100%)
Sequence domains:
Structure domains:
Metalloproteinase inhibitor 2
Molecule details ›
Chains: C, D
Length: 194 amino acids
Theoretical weight: 21.78 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains:
Length: 194 amino acids
Theoretical weight: 21.78 KDa
Source organism: Homo sapiens
Expression system: Trichoplusia ni
UniProt:
- Canonical: P16035 (Residues: 27-220; Coverage: 100%)
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains:
