Research workbench
AlphaFold monomer V2.0 prediction for thiamine import ATP-binding protein thiq (Q326G9)
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
- Q326G9
- Type
- protein
- Length
- 232 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa275367010E4cf621562A79b70DfF95f747bf221
- Molecule
- Thiamine import ATP-binding protein thiq
- UniProt
- Q326G9
- Pockets
- 2 · best druggability 0.42
Structure
1 distinct chain · 36% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thiamine import ATP-binding protein thiq | protein | 232 | 36% helix, 25% strand | Q326G9 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 111 | 0.42 | 0.76 | 14 | empty |
| 2 | 52 | 0.27 | 0.74 | 13 | 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 Q326G9
- Elsewhere: UniProt Q326G9 · AlphaFold DB Q326G9
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