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AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme (C0ZGF5)

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
C0ZGF5
Type
protein
Length
133 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x793417a5f01Ae083038547F9A7B86A2e9529e931
Molecule
S-adenosylmethionine decarboxylase proenzyme
UniProt
C0ZGF5

Structure

1 distinct chain · 25% helix, 40% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AS-adenosylmethionine decarboxylase proenzymeprotein13325% helix, 40% strandC0ZGF5

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