Research workbench
AlphaFold monomer V2.0 prediction for proline--tRNA ligase (Q5M1N3)
Analyse AlphaFold monomer V2.0 prediction for proline--tRNA ligase (Q5M1N3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5M1N3
- Type
- protein
- Length
- 620 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xD0B8f00ed836787a27f2236104D09DdB625B883a
- Molecule
- Proline--tRNA ligase
- UniProt
- Q5M1N3
- Pockets
- 4 · best druggability 0.69
Structure
1 distinct chain · 32% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline--tRNA ligase | protein | 620 | 32% helix, 30% strand | Q5M1N3 |
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 | 528 | 0.69 | 0.79 | 60 | empty |
| 2 | 182 | 0.49 | 0.77 | 25 | empty |
| 3 | 107 | 0.49 | 0.80 | 22 | empty |
| 4 | 97 | 0.35 | 0.74 | 15 | 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 Q5M1N3
- Elsewhere: UniProt Q5M1N3 · AlphaFold DB Q5M1N3
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