Research workbench
AlphaFold monomer V2.0 prediction for thioredoxin-related transmembrane protein 2 (Q9D710)
Analyse AlphaFold monomer V2.0 prediction for thioredoxin-related transmembrane protein… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9D710
- Type
- protein
- Length
- 295 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x7a1388B6Aad67B04634A32f63b8A6D6005eab86c
- Molecule
- Thioredoxin-related transmembrane protein 2
- UniProt
- Q9D710
- Pockets
- 3 · best druggability 0.66
Structure
1 distinct chain · 51% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin-related transmembrane protein 2 | protein | 295 | 51% helix, 11% strand | Q9D710 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 369 | 0.66 | 0.79 | 42 | empty |
| 2 | 341 | 0.59 | 0.77 | 31 | empty |
| 3 | 54 | 0.46 | 0.84 | 14 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q9D710
- Elsewhere: UniProt Q9D710 · AlphaFold DB Q9D710
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