Research workbench
AlphaFold monomer V2.0 prediction for elongation factor tu, mitochondrial (P49411)
Analyse AlphaFold monomer V2.0 prediction for elongation factor tu, mitochondrial… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P49411
- Type
- protein
- Length
- 452 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0xb4D2d9c96b0D792d0b77e7147D724cc1F801ae58
- UniProt
- P49411
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 452 | — | P49411 |
Compared structures
- 7A5G · Structure of the elongating human mitoribosome bound to mtEF-Tu.GMPPCP and A/T mt-tRNA · an experimental structure of the same protein · chain A against Z, TM-score 0.84
- 7O9K · Human mitochondrial ribosome large subunit assembly intermediate with MTERF4-NSUN4, MRM2… · an experimental structure of the same protein · chain A against t, TM-score 0.49
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 P49411
- Elsewhere: UniProt P49411 · AlphaFold DB P49411
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