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AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme (Q97BP8)

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
Q97BP8
Type
protein
Length
130 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x934953E3d9faD9B1cC752f4A28d5f4E6903eA0Ce
Molecule
S-adenosylmethionine decarboxylase proenzyme
UniProt
Q97BP8

Structure

1 distinct chain · 30% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AS-adenosylmethionine decarboxylase proenzymeprotein13030% helix, 38% strandQ97BP8

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