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AlphaFold monomer V2.0 prediction for segregation and condensation protein a (Q9EUR2)

Analyse AlphaFold monomer V2.0 prediction for segregation and condensation protein a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q9EUR2
Type
protein
Length
242 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xdF2b063d4B94F3f46D117B1af99A846bD4a59284
Molecule
Segregation and condensation protein a
UniProt
Q9EUR2

Structure

1 distinct chain · 58% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASegregation and condensation protein aprotein24258% helix, 5% strandQ9EUR2

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