Research workbench
AlphaFold monomer V2.0 prediction for serine--tRNA ligase (B5FQ36)
Analyse AlphaFold monomer V2.0 prediction for serine--tRNA ligase (B5FQ36) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5FQ36
- Type
- protein
- Length
- 430 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x434b0DC4af054BE165a98eb346BDbBb0889A5EB3
- Molecule
- Serine--tRNA ligase
- UniProt
- B5FQ36
- Pockets
- 4 · best druggability 0.73
Structure
1 distinct chain · 45% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Serine--tRNA ligase | protein | 430 | 45% helix, 20% strand | B5FQ36 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 603 | 0.73 | 0.81 | 52 | empty |
| 2 | 108 | 0.46 | 0.79 | 26 | empty |
| 3 | 85 | 0.39 | 0.77 | 16 | empty |
| 4 | 66 | 0.33 | 0.76 | 16 | 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 B5FQ36
- Elsewhere: UniProt B5FQ36 · AlphaFold DB B5FQ36
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