Research workbench
AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (Q5FM34)
Analyse AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (Q5FM34) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5FM34
- Type
- protein
- Length
- 477 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x70423e4d1ac346F36cee837454A0a95F42aCa410
- Molecule
- Cysteine--tRNA ligase
- UniProt
- Q5FM34
- Pockets
- 4 · best druggability 0.69
Structure
1 distinct chain · 50% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine--tRNA ligase | protein | 477 | 50% helix, 18% strand | Q5FM34 |
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 | 356 | 0.69 | 0.82 | 52 | empty |
| 2 | 216 | 0.49 | 0.75 | 28 | empty |
| 3 | 86 | 0.34 | 0.74 | 16 | empty |
| 4 | 70 | 0.32 | 0.75 | 11 | 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 Q5FM34
- Elsewhere: UniProt Q5FM34 · AlphaFold DB Q5FM34
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