Research workbench
AlphaFold monomer V2.0 prediction for eukaryotic translation initiation factor 2D (P41214)
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
- P41214
- Type
- protein
- Length
- 584 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x793417a5f01Ae083038547F9A7B86A2e9529e931
- UniProt
- P41214
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 584 | — | P41214 |
Compared structures
- 5OA3 · Human 40S-EIF2D-re-initiation complex · an experimental structure of the same protein · chain A against 0, TM-score 0.56
- 5OA9 · Human translation re-initiation complex containing EIF2D · an experimental structure of the same protein · chain A against A, TM-score 0.35
- 5OA9 · Human translation re-initiation complex containing eIF2D · an experimental structure of the same protein · chain A against A, TM-score 0.35
- 5W2F · Crystal structure of the C-terminal domain of human EIF2D at 1.4 a resolution · an experimental structure of the same protein · chain A against A, TM-score 0.34
- 5W2F · Crystal Structure of the C-terminal Domain of Human eIF2D at 1.4 A resolution · an experimental structure of the same protein · chain A against A, TM-score 0.34
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 P41214
- Elsewhere: UniProt P41214 · AlphaFold DB P41214
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