Research workbench
AlphaFold monomer V2.0 prediction for negative elongation factor D (Q5RFA0)
Analyse AlphaFold monomer V2.0 prediction for negative elongation factor D (Q5RFA0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q5RFA0
- Type
- protein
- Length
- 590 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x4Ef77Afb5a3D9F41c95Be3227D1CC986CCb61835
- Molecule
- Negative elongation factor D
- UniProt
- Q5RFA0
- Pockets
- 4 · 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 | 590 | 69% helix, 2% strand | Q5RFA0 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 642 | 0.72 | 0.79 | 51 | empty |
| 2 | 128 | 0.45 | 0.77 | 21 | empty |
| 3 | 86 | 0.39 | 0.77 | 11 | empty |
| 4 | 86 | 0.38 | 0.76 | 15 | 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 Q5RFA0
- Elsewhere: UniProt Q5RFA0 · AlphaFold DB Q5RFA0
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