Research workbench
AlphaFold monomer V2.0 prediction for elongation factor 4 (P60785)
Analyse AlphaFold monomer V2.0 prediction for elongation factor 4 (P60785) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- Accession
- P60785
- Type
- protein
- Length
- 599 residues
- Chains
- 1
- Collection
- MolNFT v1 / AlphaFold
- Contract
- 0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
- Owner
- 0x9188600a0FCa2914254C94299b1bd9721Bc4D500
- UniProt
- P60785
Structure
1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 599 | — | P60785 |
Compared structures
- 3CB4 · The Crystal Structure of LepA · an experimental structure of the same protein · chain A against D, TM-score 0.82
- 3CB4 · The crystal structure of lepa · an experimental structure of the same protein · chain A against D, TM-score 0.82
- 3JCE · Structure of Escherichia coli EF4 in pretranslocational ribosomes (Pre EF4) · an experimental structure of the same protein · chain A against x, TM-score 0.81
- 3DEG · Complex of elongating escherichia COLI 70S ribosome and EF4(LEPA)- gmppnp · an experimental structure of the same protein · chain A against C, TM-score 0.77
- 3DEG · Complex of elongating Escherichia coli 70S ribosome and EF4(LepA)-GMPPNP · an experimental structure of the same protein · chain A against C, TM-score 0.77
- 3JCD · Structure of Escherichia coli EF4 in posttranslocational ribosomes (Post EF4) · an experimental structure of the same protein · chain A against x, TM-score 0.04
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 P60785
- Elsewhere: UniProt P60785 · AlphaFold DB P60785
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