Function and Biology Details
Reaction catalysed:
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-|-Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133884 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
22 kDa interstitial collagenase
Molecule details ›
Chains: A, B, C
Length: 170 amino acids
Theoretical weight: 19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Length: 170 amino acids
Theoretical weight: 19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P03956 (Residues: 101-269; Coverage: 38%)
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Metalloproteinase inhibitor 1
Molecule details ›
Chains: D, E, F
Length: 126 amino acids
Theoretical weight: 14.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
Length: 126 amino acids
Theoretical weight: 14.27 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P01033 (Residues: 24-149; Coverage: 69%)
Sequence domains: Tissue inhibitor of metalloproteinase
Structure domains: OB fold (Dihydrolipoamide Acetyltransferase, E2P)
