Research workbench
AlphaFold monomer V2.0 prediction for thiamine import ATP-binding protein thiq (Q92L31)
Analyse AlphaFold monomer V2.0 prediction for thiamine import ATP-binding protein thiq… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q92L31
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6a3E2329d7c8AC20c4D0EC099eda7556d5C5b2b5
- Molecule
- Thiamine import ATP-binding protein thiq
- UniProt
- Q92L31
- Pockets
- 1 · best druggability 0.46
Structure
1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiamine import ATP-binding protein thiq | protein | 238 | 37% helix, 26% strand | Q92L31 |
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 | 132 | 0.46 | 0.77 | 20 | 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 Q92L31
- Elsewhere: UniProt Q92L31 · AlphaFold DB Q92L31
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