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AlphaFold monomer V2.0 prediction for thiopurine S-methyltransferase (Q5NEH3)

Analyse AlphaFold monomer V2.0 prediction for thiopurine S-methyltransferase (Q5NEH3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q5NEH3
Type
protein
Length
226 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x04fe69cF3fe65a9447FC830E38E974c3E151A82F
Molecule
Thiopurine S-methyltransferase
UniProt
Q5NEH3
Pockets
2 · best druggability 0.74

Structure

1 distinct chain · 35% helix, 23% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AThiopurine S-methyltransferaseprotein22635% helix, 23% strandQ5NEH3

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13410.740.8646empty
2660.330.7616empty

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