Research workbench
AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 3 subunit E (B3M4D9)
Analyse AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B3M4D9
- Type
- protein
- Length
- 434 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x58cbba95a543954Ec48b693257966aFbEE57af84
- Molecule
- Eukaryotic translation initiation factor 3 subunit E
- UniProt
- B3M4D9
- Pockets
- 7 · best druggability 0.58
Structure
1 distinct chain · 77% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eukaryotic translation initiation factor 3 subunit E | protein | 434 | 77% helix, 3% strand | B3M4D9 |
Pockets
7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 58 | 0.58 | 0.90 | 14 | empty |
| 2 | 202 | 0.54 | 0.78 | 23 | empty |
| 3 | 127 | 0.52 | 0.81 | 22 | empty |
| 4 | 78 | 0.42 | 0.79 | 18 | empty |
| 5 | 51 | 0.37 | 0.80 | 12 | 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 B3M4D9
- Elsewhere: UniProt B3M4D9 · AlphaFold DB B3M4D9
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