Research workbench
AlphaFold monomer V2.0 prediction for tRNA URIDINE(34) hydroxylase (A3MI14)
Analyse AlphaFold monomer V2.0 prediction for tRNA URIDINE(34) hydroxylase (A3MI14) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3MI14
- Type
- protein
- Length
- 299 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x3E987Aa5e233CDa0b5218C798Bb0c3527b9D4A2d
- Molecule
- TRNA URIDINE(34) hydroxylase
- UniProt
- A3MI14
- Pockets
- 4 · best druggability 0.65
Structure
1 distinct chain · 29% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA URIDINE(34) hydroxylase | protein | 299 | 29% helix, 23% strand | A3MI14 |
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 | 373 | 0.65 | 0.79 | 51 | empty |
| 2 | 187 | 0.59 | 0.82 | 34 | empty |
| 3 | 62 | 0.31 | 0.75 | 15 | empty |
| 4 | 52 | 0.29 | 0.75 | 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 A3MI14
- Elsewhere: UniProt A3MI14 · AlphaFold DB A3MI14
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