Research workbench
Structure of the clostridioides difficile transferase toxin
Analyse Structure of the clostridioides difficile transferase toxin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6V1S
- Type
- protein
- Length
- 2,293 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A8DS70, Q9KH42
- Ligands
- CA
Structure
electron microscopy · 6 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, F | — | protein | 272 | — | A8DS70 |
| B | — | protein | 268 | — | A8DS70 |
| C | — | protein | 265 | — | A8DS70 |
| D, G | — | protein | 273 | — | A8DS70 |
| E | — | protein | 276 | — | A8DS70 |
| Z | — | protein | 394 | — | Q9KH42 |
Ligands and binding sites
- CA · Calcium ion · metal · 14 copies · chains A, B, C, D, E, F, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6V1S · Structure of the Clostridioides difficile transferase toxin · 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 A8DS70
- Every structure of UniProt Q9KH42
- Elsewhere: RCSB PDB 6V1S · PDBe 6V1S · UniProt A8DS70 · UniProt Q9KH42
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