Research workbench
AlphaFold monomer V2.0 prediction for translation initiation factor if-2 (B5E266)
Analyse AlphaFold monomer V2.0 prediction for translation initiation factor if-2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- B5E266
- Type
- protein
- Length
- 930 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x5BeA89782341f98147F2D811B063F91F0aE7D7bF
- Molecule
- Translation initiation factor if-2
- UniProt
- B5E266
- Pockets
- 7 · best druggability 0.55
Structure
1 distinct chain · 29% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Translation initiation factor if-2 | protein | 930 | 29% helix, 23% strand | B5E266 |
Pockets
7 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 237 | 0.55 | 0.78 | 35 | empty |
| 2 | 109 | 0.49 | 0.81 | 25 | empty |
| 3 | 117 | 0.35 | 0.73 | 21 | empty |
| 4 | 91 | 0.31 | 0.72 | 23 | empty |
| 5 | 69 | 0.30 | 0.74 | 13 | 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 B5E266
- Elsewhere: UniProt B5E266 · AlphaFold DB B5E266
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