Research workbench
AlphaFold monomer V2.0 prediction for negative elongation factor D (Q922L6)
Analyse AlphaFold monomer V2.0 prediction for negative elongation factor D (Q922L6) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q922L6
- Type
- protein
- Length
- 591 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- Molecule
- Negative elongation factor D
- UniProt
- Q922L6
- Pockets
- 8 · best druggability 0.72
Structure
1 distinct chain · 69% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Negative elongation factor D | protein | 591 | 69% helix, 2% strand | Q922L6 |
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 224 | 0.72 | 0.88 | 23 | empty |
| 2 | 762 | 0.68 | 0.75 | 56 | empty |
| 3 | 141 | 0.45 | 0.76 | 26 | empty |
| 4 | 89 | 0.43 | 0.79 | 13 | empty |
| 5 | 86 | 0.43 | 0.79 | 17 | 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 Q922L6
- Elsewhere: UniProt Q922L6 · AlphaFold DB Q922L6
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