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AlphaFold monomer V2.0 prediction for stationary-phase-induced ribosome-associated protein (Q8XFL2)

Analyse AlphaFold monomer V2.0 prediction for stationary-phase-induced… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q8XFL2
Type
protein
Length
47 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x9073C46348542FfE4327c3F363F9B51B22058e75
Molecule
Stationary-phase-induced ribosome-associated protein
UniProt
Q8XFL2

Structure

1 distinct chain · 23% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AStationary-phase-induced ribosome-associated proteinprotein4723% helix, 28% strandQ8XFL2

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