Research workbench
AlphaFold monomer V2.0 prediction for tRNA 5-hydroxyuridine methyltransferase (O32036)
Analyse AlphaFold monomer V2.0 prediction for tRNA 5-hydroxyuridine methyltransferase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- O32036
- Type
- protein
- Length
- 217 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
- Molecule
- TRNA 5-hydroxyuridine methyltransferase
- UniProt
- O32036
- Pockets
- 1 · best druggability 0.55
Structure
1 distinct chain · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA 5-hydroxyuridine methyltransferase | protein | 217 | 47% helix, 20% strand | O32036 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 190 | 0.55 | 0.79 | 32 | empty |
Compared structures
- 5ZW4 · Crystal structure of tRNA bound TrmR · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 5ZW4 · Crystal structure of tRNA bound trmr · an experimental structure of the same protein · chain A against A, TM-score 0.98
- 5ZW3 · Crystal Structure of TrmR from B. subtilis · an experimental structure of the same protein · chain A against A, TM-score 0.94
- 5ZW3 · Crystal structure of trmr from B. subtilis · an experimental structure of the same protein · chain A against A, TM-score 0.94
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 O32036
- Elsewhere: UniProt O32036 · AlphaFold DB O32036
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