Research workbench
AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 3 subunit I (A6ZMK5)
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
- A6ZMK5
- Type
- protein
- Length
- 347 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x429aA010A80A47FF4a2777bB34A2bba144d19df2
- UniProt
- A6ZMK5
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 347 | — | A6ZMK5 |
Compared structures
- 4U1E · Crystal structure of the EIF3B-CTD/EIF3I/EIF3G-ntd translation initiation complex · an experimental structure of the same protein · chain A against I, TM-score 0.94
- 4U1E · Crystal structure of the eIF3b-CTD/eIF3i/eIF3g-NTD translation initiation complex · an experimental structure of the same protein · chain A against I, TM-score 0.94
- 6GSN · Structure of a partial yeast 48S preinitiation complex in closed conformation · an experimental structure of the same protein · chain A against s, TM-score 0.94
- 6FYY · Structure of a partial yeast 48S preinitiation complex with eIF5 N-terminal domain (model… · an experimental structure of the same protein · chain A against s, TM-score 0.94
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 A6ZMK5
- Elsewhere: UniProt A6ZMK5 · AlphaFold DB A6ZMK5
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