Function and Biology Details
Reaction catalysed:
Digestion of native collagen in the triple helical region at -|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1', Pro and Ala at P2 and P2', and hydroxyproline, Ala or Arg at P3'.
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domain:
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Collagenase ColG (preferred)
PDBe Complex ID:
PDB-CPX-194956 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Collagenase ColG
Molecule details ›
Chain: A
Length: 113 amino acids
Theoretical weight: 13 KDa
Source organism: Hathewaya histolytica
Expression system: Escherichia coli
UniProt:
Sequence domains: Bacterial pre-peptidase C-terminal domain
Structure domains: Jelly Rolls
Length: 113 amino acids
Theoretical weight: 13 KDa
Source organism: Hathewaya histolytica
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9X721 (Residues: 1006-1118; Coverage: 11%)
Sequence domains: Bacterial pre-peptidase C-terminal domain
Structure domains: Jelly Rolls
Collagenase ColG
Molecule details ›
Chain: B
Length: 118 amino acids
Theoretical weight: 13.51 KDa
Source organism: Hathewaya histolytica
Expression system: Escherichia coli
UniProt:
Sequence domains: Bacterial pre-peptidase C-terminal domain
Structure domains: Jelly Rolls
Length: 118 amino acids
Theoretical weight: 13.51 KDa
Source organism: Hathewaya histolytica
Expression system: Escherichia coli
UniProt:
- Canonical: Q9X721 (Residues: 1002-1118; Coverage: 11%)
Sequence domains: Bacterial pre-peptidase C-terminal domain
Structure domains: Jelly Rolls
