Research workbench
AlphaFold monomer V2.0 prediction for teichoic acids export ATP- binding protein tagh (Q2YSU3)
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
- Q2YSU3
- Type
- protein
- Length
- 264 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x0E4ca55ef0a74c0bbB9A3D5a6ddfbF71673A6a7E
- Molecule
- Teichoic acids export ATP-binding protein tagh
- UniProt
- Q2YSU3
- Pockets
- 1 · best druggability 0.31
Structure
1 distinct chain · 46% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Teichoic acids export ATP-binding protein tagh | protein | 264 | 46% helix, 27% strand | Q2YSU3 |
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 | 65 | 0.31 | 0.74 | 14 | 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 Q2YSU3
- Elsewhere: UniProt Q2YSU3 · AlphaFold DB Q2YSU3
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