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AlphaFold monomer V2.0 prediction for S-adenosylmethionine decarboxylase proenzyme (Q9I5R7)

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
Q9I5R7
Type
protein
Length
264 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x661f92Fc5950020C7aB410B5F5b9a3f429F49Ae5
Molecule
S-adenosylmethionine decarboxylase proenzyme
UniProt
Q9I5R7
Pockets
2 · best druggability 0.42

Structure

1 distinct chain · 33% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AS-adenosylmethionine decarboxylase proenzymeprotein26433% helix, 33% strandQ9I5R7

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11410.420.7523empty
2600.310.7513empty

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