Research workbench
AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (B5RMR3)
Analyse AlphaFold monomer V2.0 prediction for threonine--tRNA ligase (B5RMR3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5RMR3
- Type
- protein
- Length
- 583 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5c4adF1416281C09AE8eE1cbb80fF7e44cE86F97
- Molecule
- Threonine--tRNA ligase
- UniProt
- B5RMR3
- Pockets
- 6 · best druggability 0.68
Structure
1 distinct chain · 38% helix, 27% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Threonine--tRNA ligase | protein | 583 | 38% helix, 27% strand | B5RMR3 |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 461 | 0.68 | 0.79 | 38 | empty |
| 2 | 165 | 0.49 | 0.77 | 21 | empty |
| 3 | 56 | 0.49 | 0.85 | 18 | empty |
| 4 | 98 | 0.32 | 0.72 | 17 | empty |
| 5 | 52 | 0.29 | 0.75 | 10 | 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 B5RMR3
- Elsewhere: UniProt B5RMR3 · AlphaFold DB B5RMR3
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