Research workbench
AlphaFold monomer V2.0 prediction for proline--tRNA ligase (Q98R27)
Analyse AlphaFold monomer V2.0 prediction for proline--tRNA ligase (Q98R27) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q98R27
- Type
- protein
- Length
- 476 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Dc146208de75f433B0cA37588fA133d01B61494
- Molecule
- Proline--tRNA ligase
- UniProt
- Q98R27
- Pockets
- 4 · best druggability 0.71
Structure
1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline--tRNA ligase | protein | 476 | 36% helix, 29% strand | Q98R27 |
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 | 449 | 0.71 | 0.82 | 44 | empty |
| 2 | 111 | 0.39 | 0.75 | 19 | empty |
| 3 | 67 | 0.30 | 0.75 | 13 | empty |
| 4 | 50 | 0.28 | 0.75 | 19 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 Q98R27
- Elsewhere: UniProt Q98R27 · AlphaFold DB Q98R27
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