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AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme (P0C0A0)

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
P0C0A0
Type
protein
Length
128 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x738c1929c69B751bD0Be0B962D9bac20B631aAc6
Molecule
S-adenosylmethionine decarboxylase proenzyme
UniProt
P0C0A0

Structure

1 distinct chain · 26% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AS-adenosylmethionine decarboxylase proenzymeprotein12826% helix, 43% strandP0C0A0

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