Function and Biology Details
Reaction catalysed:
Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favored residue, which distinguished this enzyme from thermolysin.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Secreted metalloprotease Mcp02 (preferred)
PDBe Complex ID:
PDB-CPX-106589 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Secreted metalloprotease Mcp02
Molecule details ›
Chain: B
Length: 315 amino acids
Theoretical weight: 33.91 KDa
Source organism: Pseudoalteromonas sp. SM9913
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains:
Length: 315 amino acids
Theoretical weight: 33.91 KDa
Source organism: Pseudoalteromonas sp. SM9913
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
A1DRD5 (Residues: 205-519; Coverage: 45%)
Sequence domains:
Structure domains:
Secreted metalloprotease Mcp02
Molecule details ›
Chain: A
Length: 180 amino acids
Theoretical weight: 19.78 KDa
Source organism: Pseudoalteromonas sp. SM9913
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains:
Structure domains:
Length: 180 amino acids
Theoretical weight: 19.78 KDa
Source organism: Pseudoalteromonas sp. SM9913
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: A1DRD5 (Residues: 25-204; Coverage: 26%)
Sequence domains:
Structure domains:
