Research workbench
AlphaFold monomer V2.0 prediction for tRNA N6-adenosine threonylcarbamoyltransferase (A2BVD2)
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
- A2BVD2
- Type
- protein
- Length
- 356 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xd10960F956646DE8b64d3598984c91C2d5Af3D7b
- Molecule
- TRNA N6-adenosine threonylcarbamoyltransferase
- UniProt
- A2BVD2
- Pockets
- 3 · best druggability 0.66
Structure
1 distinct chain · 46% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA N6-adenosine threonylcarbamoyltransferase | protein | 356 | 46% helix, 20% strand | A2BVD2 |
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 | 432 | 0.66 | 0.79 | 43 | empty |
| 2 | 64 | 0.42 | 0.81 | 19 | empty |
| 3 | 73 | 0.32 | 0.75 | 17 | 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 A2BVD2
- Elsewhere: UniProt A2BVD2 · AlphaFold DB A2BVD2
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