Research workbench
AlphaFold monomer V2.0 prediction for tRNA pseudouridine synthase a (A7FGM1)
Analyse AlphaFold monomer V2.0 prediction for tRNA pseudouridine synthase a (A7FGM1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A7FGM1
- Type
- protein
- Length
- 264 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1BC1aba9D40716Daa3370FdFC773ded2A507685C
- Molecule
- TRNA pseudouridine synthase a
- UniProt
- A7FGM1
- Pockets
- 4 · best druggability 0.62
Structure
1 distinct chain · 24% helix, 28% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA pseudouridine synthase a | protein | 264 | 24% helix, 28% strand | A7FGM1 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 335 | 0.62 | 0.79 | 35 | empty |
| 2 | 145 | 0.52 | 0.80 | 26 | empty |
| 3 | 72 | 0.32 | 0.75 | 17 | empty |
| 4 | 57 | 0.27 | 0.73 | 15 | 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 A7FGM1
- Elsewhere: UniProt A7FGM1 · AlphaFold DB A7FGM1
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