Research workbench
AlphaFold monomer V2.0 prediction for proline--tRNA ligase (Q038L9)
Analyse AlphaFold monomer V2.0 prediction for proline--tRNA ligase (Q038L9) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q038L9
- Type
- protein
- Length
- 575 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBd1df4520bd720D8bA9c973740d544444e1D22F2
- Molecule
- Proline--tRNA ligase
- UniProt
- Q038L9
- Pockets
- 4 · best druggability 0.69
Structure
1 distinct chain · 31% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline--tRNA ligase | protein | 575 | 31% helix, 30% strand | Q038L9 |
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 593 | 0.69 | 0.78 | 66 | empty |
| 2 | 117 | 0.51 | 0.81 | 21 | empty |
| 3 | 84 | 0.45 | 0.81 | 19 | empty |
| 4 | 53 | 0.30 | 0.76 | 13 | 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 Q038L9
- Elsewhere: UniProt Q038L9 · AlphaFold DB Q038L9
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