Research workbench
AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 3 subunit B (Q6FM92)
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
- Q6FM92
- Type
- protein
- Length
- 719 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x01C017170E73d5c19B7fb5953033733C6E5Cad10
- Molecule
- Eukaryotic translation initiation factor 3 subunit B
- UniProt
- Q6FM92
- Pockets
- 8 · best druggability 0.64
Structure
1 distinct chain · 16% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eukaryotic translation initiation factor 3 subunit B | protein | 719 | 16% helix, 35% strand | Q6FM92 |
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 | 777 | 0.64 | 0.73 | 79 | empty |
| 2 | 212 | 0.51 | 0.76 | 24 | empty |
| 3 | 201 | 0.48 | 0.75 | 21 | empty |
| 4 | 75 | 0.37 | 0.77 | 17 | empty |
| 5 | 76 | 0.32 | 0.74 | 16 | 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 Q6FM92
- Elsewhere: UniProt Q6FM92 · AlphaFold DB Q6FM92
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