MolNFT v1 · #111636 · protein
AlphaFold monomer V2.0 prediction for elongation factor G (Q4FQG5)
Q4FQG5: “AlphaFold monomer V2.0 prediction for elongation factor G (Q4FQG5)”. 6 pockets (best druggability 0.61). MolNFT v1 #111636 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- Accession
- Q4FQG5
- Type
- protein
- Length
- 708 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9fd4A2A02913F236a68052054387e7b782a8d58e
- Molecule
- Elongation factor G
- UniProt
- Q4FQG5
- Pockets
- 6 · best druggability 0.61
Structure
1 distinct chain · 31% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor G | protein | 708 | 31% helix, 32% strand | Q4FQG5 |
Pockets
6 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 215 | 0.61 | 0.81 | 31 | empty |
| 2 | 281 | 0.59 | 0.78 | 24 | empty |
| 3 | 106 | 0.57 | 0.85 | 25 | empty |
| 4 | 207 | 0.55 | 0.78 | 27 | empty |
| 5 | 243 | 0.53 | 0.76 | 32 | 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 Q4FQG5
- Elsewhere: UniProt Q4FQG5 · AlphaFold DB Q4FQG5
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