Research workbench
AlphaFold monomer V2.0 prediction for proline--tRNA ligase (B5R434)
Analyse AlphaFold monomer V2.0 prediction for proline--tRNA ligase (B5R434) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5R434
- Type
- protein
- Length
- 572 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x78Cc7f9BF18AF8279e492D45EE7Fe9d7cC6f6D07
- Molecule
- Proline--tRNA ligase
- UniProt
- B5R434
- Pockets
- 3 · best druggability 0.72
Structure
1 distinct chain · 29% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline--tRNA ligase | protein | 572 | 29% helix, 29% strand | B5R434 |
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 | 511 | 0.72 | 0.81 | 46 | empty |
| 2 | 98 | 0.42 | 0.77 | 23 | empty |
| 3 | 65 | 0.29 | 0.73 | 18 | 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 B5R434
- Elsewhere: UniProt B5R434 · AlphaFold DB B5R434
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