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 P15917
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)
P15917 |
LEF_BACAN
Bacillus anthracis
Lethal factor
|
PDB Structure
PDB | 4WF6 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Probing the S2' Subsite of the Anthrax Toxin Lethal Factor Using Novel N-Alkylated Hydroxamates.
J.Med.Chem.
|