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AlphaFold monomer V2.0 prediction for tRNA-CYTIDINE(32) 2-sulfurtransferase (Q92PH1)
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
- Q92PH1
- Type
- protein
- Length
- 294 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xF4bb4e5FAc04d8727C4ae3523172c2f5b40A2130
- Molecule
- TRNA-CYTIDINE(32) 2-sulfurtransferase
- UniProt
- Q92PH1
- Pockets
- 3 · best druggability 0.76
Structure
1 distinct chain · 44% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA-CYTIDINE(32) 2-sulfurtransferase | protein | 294 | 44% helix, 9% strand | Q92PH1 |
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 | 760 | 0.76 | 0.80 | 60 | empty |
| 2 | 95 | 0.35 | 0.74 | 17 | empty |
| 3 | 58 | 0.30 | 0.75 | 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 Q92PH1
- Elsewhere: UniProt Q92PH1 · AlphaFold DB Q92PH1
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