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AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme (Q5KWC6)

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
Q5KWC6
Type
protein
Length
124 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x404dD93cd2E0F7C9B647A7c82A4C1aCbcc756C0A
Molecule
S-adenosylmethionine decarboxylase proenzyme
UniProt
Q5KWC6

Structure

1 distinct chain · 27% helix, 42% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AS-adenosylmethionine decarboxylase proenzymeprotein12427% helix, 42% strandQ5KWC6

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