Research workbench
AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (C5BI15)
Analyse AlphaFold monomer V2.0 prediction for cysteine--tRNA ligase (C5BI15) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- C5BI15
- Type
- protein
- Length
- 458 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x1ED4a68B4011314730adE976b56Ad4cA21b54dcD
- Molecule
- Cysteine--tRNA ligase
- UniProt
- C5BI15
- Pockets
- 4 · best druggability 0.66
Structure
1 distinct chain · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Cysteine--tRNA ligase | protein | 458 | 48% helix, 16% strand | C5BI15 |
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 | 326 | 0.66 | 0.81 | 36 | empty |
| 2 | 156 | 0.44 | 0.75 | 31 | empty |
| 3 | 107 | 0.37 | 0.74 | 21 | empty |
| 4 | 68 | 0.36 | 0.77 | 17 | 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 C5BI15
- Elsewhere: UniProt C5BI15 · AlphaFold DB C5BI15
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