Research workbench
AlphaFold monomer V2.0 prediction for proline--tRNA ligase, CHLOROPLASTIC/MITOCHONDRIAL (Q9FYR6)
Analyse AlphaFold monomer V2.0 prediction for proline--tRNA ligase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q9FYR6
- Type
- protein
- Length
- 543 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xAB101f7Cfd0D22Bf85F642916550b92ff64174f9
- Molecule
- Proline--tRNA ligase, CHLOROPLASTIC/MITOCHONDRIAL
- UniProt
- Q9FYR6
- Pockets
- 3 · best druggability 0.71
Structure
1 distinct chain · 36% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline--tRNA ligase, CHLOROPLASTIC/MITOCHONDRIAL | protein | 543 | 36% helix, 26% strand | Q9FYR6 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 419 | 0.71 | 0.82 | 42 | empty |
| 2 | 182 | 0.47 | 0.76 | 24 | empty |
| 3 | 87 | 0.34 | 0.74 | 20 | 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 Q9FYR6
- Elsewhere: UniProt Q9FYR6 · AlphaFold DB Q9FYR6
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