Research workbench
AlphaFold monomer V2.0 prediction for thioredoxin-related transmembrane protein 2 homolog (Q18484)
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
- Q18484
- Type
- protein
- Length
- 265 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd91633319BDB0a92cbC4f08DeA734Bf74C030064
- Molecule
- Thioredoxin-related transmembrane protein 2 homolog
- UniProt
- Q18484
- Pockets
- 3 · best druggability 0.62
Structure
1 distinct chain · 56% helix, 12% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin-related transmembrane protein 2 homolog | protein | 265 | 56% helix, 12% strand | Q18484 |
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 | 203 | 0.62 | 0.83 | 26 | empty |
| 2 | 321 | 0.58 | 0.76 | 39 | empty |
| 3 | 76 | 0.41 | 0.79 | 18 | 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 Q18484
- Elsewhere: UniProt Q18484 · AlphaFold DB Q18484
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