Research workbench
AlphaFold monomer V2.0 prediction for tRNA N6-adenosine threonylcarbamoyltransferase (B2S3R9)
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
- B2S3R9
- Type
- protein
- Length
- 352 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xC7cc4fC1fc1b08Ba48e6eA6ee8b27b213776B21D
- Molecule
- TRNA N6-adenosine threonylcarbamoyltransferase
- UniProt
- B2S3R9
- Pockets
- 3 · best druggability 0.68
Structure
1 distinct chain · 47% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | TRNA N6-adenosine threonylcarbamoyltransferase | protein | 352 | 47% helix, 19% strand | B2S3R9 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 435 | 0.68 | 0.80 | 46 | empty |
| 2 | 177 | 0.51 | 0.77 | 21 | empty |
| 3 | 51 | 0.23 | 0.72 | 13 | 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 B2S3R9
- Elsewhere: UniProt B2S3R9 · AlphaFold DB B2S3R9
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