Research workbench
Clostridium perfringens epsilon toxin shows structural similarity with the pore forming toxin aerolysin
Analyse Clostridium perfringens epsilon toxin shows structural similarity with the pore… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1UYJ
- Type
- protein
- Length
- 819 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Epsilon-toxin
- UniProt
- Q57398
- Ligands
- U1
Structure
x-ray diffraction · 1 distinct chain · 10% helix, 55% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Epsilon-toxin | protein | 273 | 10% helix, 55% strand | Q57398 |
Ligands and binding sites
- U1 · Uranium atom · metal · 12 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1UYJ · Clostridium perfringens epsilon toxin shows structural similarity with the pore forming… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q57398
- Elsewhere: RCSB PDB 1UYJ · PDBe 1UYJ · UniProt Q57398
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