Research workbench
AlphaFold monomer V2.0 prediction for glutamate--tRNA ligase (B5RCP1)
Analyse AlphaFold monomer V2.0 prediction for glutamate--tRNA ligase (B5RCP1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5RCP1
- Type
- protein
- Length
- 471 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBeB220F0B5b0C48F46B5DDd3E3b071BC0827f8D6
- Molecule
- Glutamate--tRNA ligase
- UniProt
- B5RCP1
- Pockets
- 3 · best druggability 0.69
Structure
1 distinct chain · 52% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutamate--tRNA ligase | protein | 471 | 52% helix, 13% strand | B5RCP1 |
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 | 289 | 0.69 | 0.84 | 33 | empty |
| 2 | 156 | 0.41 | 0.74 | 27 | empty |
| 3 | 72 | 0.30 | 0.74 | 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 B5RCP1
- Elsewhere: UniProt B5RCP1 · AlphaFold DB B5RCP1
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