Research workbench
AlphaFold monomer V2.0 prediction for elongation factor 2 (P23112)
Analyse AlphaFold monomer V2.0 prediction for elongation factor 2 (P23112) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P23112
- Type
- protein
- Length
- 737 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x6Ed09D80e98fE15DE51C9E7a8896AbF1f2365C3e
- UniProt
- P23112
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 737 | — | P23112 |
Compared structures
- 8HL4 · Cryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosome · an experimental structure of the same protein · chain A against AEFG, TM-score 0.68
- 8HL2 · Cryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosome · an experimental structure of the same protein · chain A against AEFG, TM-score 0.67
- 8HL3 · Cryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosome · an experimental structure of the same protein · chain A against AEFG, TM-score 0.67
- 8HL1 · Cryo-EM Structures and Translocation Mechanism of Crenarchaeota Ribosome · an experimental structure of the same protein · chain A against AEFG, TM-score 0.67
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 P23112
- Elsewhere: UniProt P23112 · AlphaFold DB P23112
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