CATH Classification
Level | CATH Code | Description |
---|---|---|
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3 | Alpha Beta |
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3.90 | Alpha-Beta Complex |
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3.90.176 | Toxin ADP-ribosyltransferase; Chain A, domain 1 |
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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.
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UniProtKB Entries (1)
P15917 |
LEF_BACAN
Bacillus anthracis
Lethal factor
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PDB Structure
PDB | 4XM6 |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Ligand-induced expansion of the S1' site in the anthrax toxin lethal factor.
Febs Lett.
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