Research workbench
AlphaFold monomer V2.0 prediction for tRNA N6-adenosine threonylcarbamoyltransferase (A2RI22)
Analyse AlphaFold monomer V2.0 prediction for tRNA N6-adenosine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A2RI22
- Type
- protein
- Length
- 341 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb0eE012d633aaaddC45C81d2C278B0cA4d9F1ec5
- Molecule
- TRNA N6-adenosine threonylcarbamoyltransferase
- UniProt
- A2RI22
- Pockets
- 2 · best druggability 0.68
Structure
1 distinct chain · 48% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA N6-adenosine threonylcarbamoyltransferase | protein | 341 | 48% helix, 18% strand | A2RI22 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 496 | 0.68 | 0.79 | 48 | empty |
| 2 | 64 | 0.36 | 0.78 | 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 A2RI22
- Elsewhere: UniProt A2RI22 · AlphaFold DB A2RI22
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