Function and Biology Details
Reaction catalysed:
Preferred amino acids around the cleavage site can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases.
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Lethal factor (preferred)
PDBe Complex ID:
PDB-CPX-147525 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lethal factor
Molecule details ›
Chain: A
Length: 106 amino acids
Theoretical weight: 12.14 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli BL21
UniProt:
Sequence domains: Anthrax toxin lethal factor, N- and C-terminal domain
Structure domains: Collagenase (Catalytic Domain)
Length: 106 amino acids
Theoretical weight: 12.14 KDa
Source organism: Bacillus anthracis
Expression system: Escherichia coli BL21
UniProt:
- Canonical:
P15917 (Residues: 705-809; Coverage: 14%)
Sequence domains: Anthrax toxin lethal factor, N- and C-terminal domain
Structure domains: Collagenase (Catalytic Domain)
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
Refinement method:
Molexular mechanics
Expression system: Escherichia coli BL21
