GL1X · GenesisL1 explorer

UniProt Q9KH42

ADP-ribosylating binary toxin enzymatic subunit CdtA (Q9KH42)

ADP-ribosylating binary toxin enzymatic subunit CdtA (UniProt Q9KH42), EC 2.4.2.-: 16 experimental structures on GenesisL1, 28 pockets. Binding sites, pockets, druggability and 3D structures in GL1X.

UniProt
Q9KH42
Protein
ADP-ribosylating binary toxin enzymatic subunit CdtA
EC
2.4.2.-
Experimental structures
16
Predicted models
0
Pockets
28 · 5 records with a druggable one

Structures

16 records of Q9KH42 in the MolNFT archive: 16 experimental, 0 predicted.

EntryTitleMethodChainsLigandsPockets
2WN4Structural Basis for Substrate Recognition in the Enzymatic Component of ADP-ribosyltransferase…x-ray diffractionA——
2WN4Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase…x-ray diffractionA——
2WN5Structural Basis for Substrate Recognition in the Enzymatic Component of ADP-ribosyltransferase…x-ray diffractionA——
2WN5Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase…x-ray diffractionA——
2WN6Structural Basis for Substrate Recognition in the Enzymatic Component of ADP-ribosyltransferase…x-ray diffractionA——
2WN6Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase…x-ray diffractionA——
2WN7Structural Basis for Substrate Recognition in the Enzymatic Component of ADP-ribosyltransferase…x-ray diffractionA——
2WN7Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase…x-ray diffractionA——
2WN8Structural Basis for Substrate Recognition in the Enzymatic Component of ADP-ribosyltransferase…x-ray diffractionA——
2WN8Structural basis for substrate recognition in the enzymatic component of ADP-ribosyltransferase…x-ray diffractionA——
6V1SStructure of the Clostridioides difficile transferase toxinelectron microscopyZ—6 (best 0.83)
6V1SStructure of the clostridioides difficile transferase toxinelectron microscopyZ——
7VNJComplex structure of Clostridioides difficile enzymatic component (CDTa) and binding component…electron microscopyH—6 (best 0.83)
7YVQComplex structure of Clostridioides difficile binary toxin folded CDTa-bound CDTb-pore (short).electron microscopyH—5 (best 0.86)
7YVSComplex structure of Clostridioides difficile binary toxin unfolded CDTa-bound CDTb-pore (short).electron microscopyH—7 (best 0.86)
9BBFStructure of Clostridioides difficile Component A (50-463) in Complex with a CDTb Oligomerelectron microscopyZ—4 (best 0.86)

Elsewhere

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.