Research workbench
AlphaFold monomer V2.0 prediction for thioredoxin Y, chloroplastic (Q5JMR9)
Analyse AlphaFold monomer V2.0 prediction for thioredoxin Y, chloroplastic (Q5JMR9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5JMR9
- Type
- protein
- Length
- 168 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF336F3B74E376B91b0149E66DCdF03429c696250
- Molecule
- Thioredoxin Y, chloroplastic
- UniProt
- Q5JMR9
- Pockets
- 2 · best druggability 0.29
Structure
1 distinct chain · 26% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Thioredoxin Y, chloroplastic | protein | 168 | 26% helix, 15% strand | Q5JMR9 |
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 | 54 | 0.29 | 0.74 | 11 | empty |
| 2 | 66 | 0.27 | 0.72 | 12 | 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 Q5JMR9
- Elsewhere: UniProt Q5JMR9 · AlphaFold DB Q5JMR9
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.