Research workbench
AlphaFold monomer V2.0 prediction for proline--tRNA ligase (A3PBN3)
Analyse AlphaFold monomer V2.0 prediction for proline--tRNA ligase (A3PBN3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A3PBN3
- Type
- protein
- Length
- 600 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Proline--tRNA ligase
- UniProt
- A3PBN3
- Pockets
- 4 · best druggability 0.77
Structure
1 distinct chain · 30% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Proline--tRNA ligase | protein | 600 | 30% helix, 29% strand | A3PBN3 |
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 | 908 | 0.77 | 0.80 | 76 | empty |
| 2 | 147 | 0.56 | 0.82 | 24 | empty |
| 3 | 93 | 0.38 | 0.76 | 22 | empty |
| 4 | 55 | 0.29 | 0.75 | 15 | empty |
Modifications
Observed in the structure: 1 disulfide (disulfide).
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 A3PBN3
- Elsewhere: UniProt A3PBN3 · AlphaFold DB A3PBN3
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