Research workbench
AlphaFold monomer V2.0 prediction for methionine--tRNA ligase (B5YV64)
Analyse AlphaFold monomer V2.0 prediction for methionine--tRNA ligase (B5YV64) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5YV64
- Type
- protein
- Length
- 677 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x357494D6985DbB6d0e40B74Bc031C05d59768EB4
- Molecule
- Methionine--tRNA ligase
- UniProt
- B5YV64
- Pockets
- 3 · best druggability 0.63
Structure
1 distinct chain · 44% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methionine--tRNA ligase | protein | 677 | 44% helix, 20% strand | B5YV64 |
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 | 267 | 0.63 | 0.81 | 30 | empty |
| 2 | 198 | 0.47 | 0.74 | 30 | empty |
| 3 | 51 | 0.26 | 0.74 | 19 | 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 B5YV64
- Elsewhere: UniProt B5YV64 · AlphaFold DB B5YV64
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