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AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme (A6UQM8)

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

Accession
A6UQM8
Type
protein
Length
122 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0xaB789Baa1a4cC08f183fc9B31E29805Ea05FE2FC
Molecule
S-adenosylmethionine decarboxylase proenzyme
UniProt
A6UQM8

Structure

1 distinct chain · 31% helix, 46% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AS-adenosylmethionine decarboxylase proenzymeprotein12231% helix, 46% strandA6UQM8

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