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AlphaFold monomer V2.0 prediction for tRNA-CYTIDINE(32) 2-sulfurtransferase 1 (Q14HG9)
Analyse AlphaFold monomer V2.0 prediction for tRNA-CYTIDINE(32) 2-sulfurtransferase 1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q14HG9
- Type
- protein
- Length
- 267 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5Cc8336db6d496E3B01007Aa23AcE4A695b4613E
- Molecule
- TRNA-CYTIDINE(32) 2-sulfurtransferase 1
- UniProt
- Q14HG9
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 47% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA-CYTIDINE(32) 2-sulfurtransferase 1 | protein | 267 | 47% helix, 10% strand | Q14HG9 |
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 | 704 | 0.69 | 0.77 | 63 | empty |
| 2 | 108 | 0.39 | 0.75 | 24 | empty |
| 3 | 65 | 0.32 | 0.75 | 13 | 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 Q14HG9
- Elsewhere: UniProt Q14HG9 · AlphaFold DB Q14HG9
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