Research workbench
AlphaFold monomer V2.0 prediction for translation initiation factor eif-2B subunit epsilon (Q13144)
Analyse AlphaFold monomer V2.0 prediction for translation initiation factor eif-2B… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- Q13144
- Type
- protein
- Length
- 721 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xa73BAb1DabE4333A884D03393eAa10c3B4215494
- UniProt
- Q13144
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 721 | — | Q13144 |
Compared structures
- 6O85 · Electron cryo-microscopy of the eukaryotic translation initiation factor 2B bound to… · an experimental structure of the same protein · chain A against B, TM-score 0.61
- 6O85 · Electron cryo-microscopy of the eukaryotic translation initiation factor 2B bound to… · an experimental structure of the same protein · chain A against B, TM-score 0.61
- 6O81 · Electron cryo-microscopy of the eukaryotic translation initiation factor 2B bound to… · an experimental structure of the same protein · chain A against A, TM-score 0.61
- 6O81 · Electron cryo-microscopy of the eukaryotic translation initiation factor 2B bound to… · an experimental structure of the same protein · chain A against A, TM-score 0.61
- 7F66 · EIF2B-sfsv nss-1-EIF2 · an experimental structure of the same protein · chain A against J, TM-score 0.61
- 7F66 · eIF2B-SFSV NSs-1-eIF2 · an experimental structure of the same protein · chain A against J, TM-score 0.61
- 7F67 · EIF2B-sfsv nss-2-EIF2 · an experimental structure of the same protein · chain A against I, TM-score 0.61
- 7F67 · eIF2B-SFSV NSs-2-eIF2 · an experimental structure of the same protein · chain A against I, TM-score 0.61
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 Q13144
- Elsewhere: UniProt Q13144 · AlphaFold DB Q13144
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