Research workbench
AlphaFold monomer V2.0 prediction for glutamine--tRNA ligase (C1DHE5)
Analyse AlphaFold monomer V2.0 prediction for glutamine--tRNA ligase (C1DHE5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C1DHE5
- Type
- protein
- Length
- 555 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- Molecule
- Glutamine--tRNA ligase
- UniProt
- C1DHE5
- Pockets
- 5 · best druggability 0.76
Structure
1 distinct chain · 29% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamine--tRNA ligase | protein | 555 | 29% helix, 26% strand | C1DHE5 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 118 | 0.76 | 0.95 | 29 | empty |
| 2 | 326 | 0.69 | 0.82 | 26 | empty |
| 3 | 87 | 0.46 | 0.81 | 17 | empty |
| 4 | 71 | 0.38 | 0.79 | 17 | empty |
| 5 | 117 | 0.38 | 0.74 | 22 | 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 C1DHE5
- Elsewhere: UniProt C1DHE5 · AlphaFold DB C1DHE5
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