CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.176 | Toxin ADP-ribosyltransferase; Chain A, domain 1 |
|
3.90.176.10 | Toxin ADP-ribosyltransferase; Chain A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | Toxin ADP-ribosyltransferase; Chain A, domain 1 |
| Functional Family |
Enzyme Information
| 3.4.24.83 |
Anthrax lethal factor endopeptidase.
based on mapping to UniProt Q52NH3
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.
-!- From the bacterium Bacilus anthracis that causes anthrax. -!- One of three proteins that are collectively termed anthrax toxin. -!- Cleaves several MAP kinase kinases near their N-termini, preventing them from phosphorylating the downstream mitogen-activated protein kinases. -!- Belongs to peptidase family M34.
|
UniProtKB Entries (1)
| Q52NH3 |
Q52NH3_BACAN
Bacillus anthracis
Lethal factor
|
PDB Structure
| PDB | 1ZXV |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Bacillus |
| Primary Citation |
Efficient synthetic inhibitors of anthrax lethal factor.
Proc.Natl.Acad.Sci.Usa
|
