Research workbench
AlphaFold monomer V2.0 prediction for elongation factor ts (P43895)
Analyse AlphaFold monomer V2.0 prediction for elongation factor ts (P43895) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P43895
- Type
- protein
- Length
- 196 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x88266F45E0832E38C9d906b86a6EE2d52e9cb6cC
- UniProt
- P43895
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 196 | — | P43895 |
Compared structures
- 1AIP · Ef-tu ef-ts complex from thermus thermophilus · an experimental structure of the same protein · chain A against C, TM-score 0.95
- 1AIP · Ef-tu ef-ts complex from thermus thermophilus · an experimental structure of the same protein · chain A against C, TM-score 0.95
- 1TFE · Dimerization domain of ef-ts from T. thermophilus · an experimental structure of the same protein · chain A against A, TM-score 0.71
- 1TFE · Dimerization domain of ef-ts from T. thermophilus · an experimental structure of the same protein · chain A against A, TM-score 0.71
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 P43895
- Elsewhere: UniProt P43895 · AlphaFold DB P43895
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