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AlphaFold monomer V2.0 prediction for glycine--tRNA ligase alpha subunit (A4XN73)
Analyse AlphaFold monomer V2.0 prediction for glycine--tRNA ligase alpha subunit… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A4XN73
- Type
- protein
- Length
- 315 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5e58272ea25a05e06901A2eAe9f63939b344e0c6
- Molecule
- Glycine--tRNA ligase alpha subunit
- UniProt
- A4XN73
- Pockets
- 3 · best druggability 0.67
Structure
1 distinct chain · 46% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glycine--tRNA ligase alpha subunit | protein | 315 | 46% helix, 23% strand | A4XN73 |
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 | 402 | 0.67 | 0.80 | 42 | empty |
| 2 | 89 | 0.39 | 0.77 | 13 | empty |
| 3 | 59 | 0.32 | 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 A4XN73
- Elsewhere: UniProt A4XN73 · AlphaFold DB A4XN73
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