Research workbench
Structure of cdtb, the biologically active subunit of cytolethal distending toxin
Analyse Structure of cdtb, the biologically active subunit of cytolethal distending… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2F1N
- Type
- protein
- Length
- 253 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Cytolethal distending toxin subunit B
- UniProt
- Q46669
- Pockets
- 1 · best druggability 0.35
Structure
x-ray diffraction · 1 distinct chain · 17% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cytolethal distending toxin subunit B | protein | 253 | 17% helix, 32% strand | Q46669 |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 51 | 0.35 | 0.79 | 14 | empty |
Compared structures
- 2F1N · Structure of CdtB, the biologically active subunit of Cytolethal Distending Toxin · the same entry in another collection · chain A against A, TM-score 1.00
- Q46669 · AlphaFold monomer V2.0 prediction for cytolethal distending toxin subunit B (Q46669) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q46669
- Elsewhere: RCSB PDB 2F1N · PDBe 2F1N · UniProt Q46669
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