Research workbench
AlphaFold monomer V2.0 prediction for elongation factor tu (A0QS98)
Analyse AlphaFold monomer V2.0 prediction for elongation factor tu (A0QS98) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- A0QS98
- Type
- protein
- Length
- 396 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xBE81563aE073ce9CCBbFCd4eb1F3935F14a0001F
- UniProt
- A0QS98
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 396 | — | A0QS98 |
Compared structures
- 8V9L · Cryo-EM structure of the Mycobacterium smegmatis 70S ribosome in complex with hibernation… · an experimental structure of the same protein · chain A against x, TM-score 0.57
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 A0QS98
- Elsewhere: UniProt A0QS98 · AlphaFold DB A0QS98
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