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AlphaFold monomer V2.0 prediction for tRNA-CYTIDINE(32) 2-sulfurtransferase (A5IGL1)
Analyse AlphaFold monomer V2.0 prediction for tRNA-CYTIDINE(32) 2-sulfurtransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A5IGL1
- Type
- protein
- Length
- 283 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x744CdE2c0e41F74D7F5Aef2e7116425c8499d7f4
- Molecule
- TRNA-CYTIDINE(32) 2-sulfurtransferase
- UniProt
- A5IGL1
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 47% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA-CYTIDINE(32) 2-sulfurtransferase | protein | 283 | 47% helix, 10% strand | A5IGL1 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 770 | 0.72 | 0.78 | 64 | empty |
| 2 | 53 | 0.33 | 0.77 | 13 | empty |
| 3 | 50 | 0.30 | 0.76 | 14 | 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 A5IGL1
- Elsewhere: UniProt A5IGL1 · AlphaFold DB A5IGL1
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