Research workbench
AlphaFold monomer V2.0 prediction for proline--tRNA ligase (B8G3V5)
Analyse AlphaFold monomer V2.0 prediction for proline--tRNA ligase (B8G3V5) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B8G3V5
- Type
- protein
- Length
- 480 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- Molecule
- Proline--tRNA ligase
- UniProt
- B8G3V5
- Pockets
- 4 · best druggability 0.70
Structure
1 distinct chain · 36% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline--tRNA ligase | protein | 480 | 36% helix, 29% strand | B8G3V5 |
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 | 426 | 0.70 | 0.82 | 45 | empty |
| 2 | 107 | 0.39 | 0.75 | 15 | empty |
| 3 | 83 | 0.33 | 0.74 | 12 | empty |
| 4 | 52 | 0.32 | 0.77 | 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 B8G3V5
- Elsewhere: UniProt B8G3V5 · AlphaFold DB B8G3V5
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