Research workbench
AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (C1FK28)
Analyse AlphaFold monomer V2.0 prediction for arginine--tRNA ligase (C1FK28) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C1FK28
- Type
- protein
- Length
- 563 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x97EfFf2d74994e28D3b69b1503Bd9c292B2Df480
- Molecule
- Arginine--tRNA ligase
- UniProt
- C1FK28
- Pockets
- 4 · best druggability 0.62
Structure
1 distinct chain · 59% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Arginine--tRNA ligase | protein | 563 | 59% helix, 11% strand | C1FK28 |
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 425 | 0.62 | 0.77 | 48 | empty |
| 2 | 67 | 0.61 | 0.91 | 17 | empty |
| 3 | 238 | 0.56 | 0.78 | 36 | empty |
| 4 | 65 | 0.30 | 0.75 | 15 | 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 C1FK28
- Elsewhere: UniProt C1FK28 · AlphaFold DB C1FK28
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