Research workbench
AlphaFold monomer V2.0 prediction for teichoic acids export ATP- binding protein tagh (Q8Y843)
Analyse AlphaFold monomer V2.0 prediction for teichoic acids export ATP- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q8Y843
- Type
- protein
- Length
- 333 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x71112d4fF7ebb3b617963c05f052289e073082FD
- Molecule
- Teichoic acids export ATP-binding protein tagh
- UniProt
- Q8Y843
- Pockets
- 3 · best druggability 0.48
Structure
1 distinct chain · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Teichoic acids export ATP-binding protein tagh | protein | 333 | 45% helix, 20% strand | Q8Y843 |
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 269 | 0.48 | 0.73 | 36 | empty |
| 2 | 85 | 0.46 | 0.81 | 19 | empty |
| 3 | 53 | 0.25 | 0.72 | 18 | empty |
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 Q8Y843
- Elsewhere: UniProt Q8Y843 · AlphaFold DB Q8Y843
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