Research workbench
AlphaFold monomer V2.0 prediction for elongation factor tu (P52854)
Analyse AlphaFold monomer V2.0 prediction for elongation factor tu (P52854) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P52854
- Type
- protein
- Length
- 410 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xbDA05C32aD6eE153C8C5A78dfa48d7Ba25694fea
- Molecule
- Elongation factor tu
- UniProt
- P52854
- Pockets
- 6 · best druggability 0.66
Structure
1 distinct chain · 23% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor tu | protein | 410 | 23% helix, 37% strand | P52854 |
Pockets
6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 449 | 0.66 | 0.78 | 43 | empty |
| 2 | 369 | 0.60 | 0.77 | 45 | empty |
| 3 | 159 | 0.54 | 0.80 | 33 | empty |
| 4 | 74 | 0.35 | 0.76 | 12 | empty |
| 5 | 71 | 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 P52854
- Elsewhere: UniProt P52854 · AlphaFold DB P52854
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