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 ›
Chain: A
Length: 168 amino acids
Theoretical weight: 18.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Length: 168 amino acids
Theoretical weight: 18.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P08254 (Residues: 100-267; Coverage: 37%)
Sequence domains: Matrixin
Structure domains: Collagenase (Catalytic Domain)
Metalloproteinase inhibitor 1
Molecule details ›
Chain: B
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)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
RIGID BODY MINIMIZATION FOLLOWED BY RESTRAINED SIMULATED ANNEALING
Expression system: Escherichia coli BL21(DE3)
