Function and Biology Details
Reaction catalysed:
Preferential cleavage in proteins: -Xaa-|-Lys- (in which Xaa may be Pro).
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Peptidyl-Lys metalloendopeptidase (preferred)
PDBe Complex ID:
PDB-CPX-160476 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-Lys metalloendopeptidase
Molecule details ›
Chains: A, B
Length: 167 amino acids
Theoretical weight: 18.06 KDa
Source organism: Grifola frondosa
UniProt:
Sequence domains: Lysine-specific metallo-endopeptidase
Structure domains: Collagenase (Catalytic Domain)
Length: 167 amino acids
Theoretical weight: 18.06 KDa
Source organism: Grifola frondosa
UniProt:
- Canonical:
P81054 (Residues: 182-348; Coverage: 51%)
Sequence domains: Lysine-specific metallo-endopeptidase
Structure domains: Collagenase (Catalytic Domain)
