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AlphaFold monomer V2.0 prediction for ethanol acetyltransferase 1 (A0A1E4S2P1)

Analyse AlphaFold monomer V2.0 prediction for ethanol acetyltransferase 1 (A0A1E4S2P1) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
A0A1E4S2P1
Type
protein
Length
336 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x7b6a4c677791A9A6a0559511958AA45768d4d8ee
Molecule
Ethanol acetyltransferase 1
Pockets
6 · best druggability 0.68

Structure

1 distinct chain · 38% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEthanol acetyltransferase 1protein33638% helix, 13% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12870.680.8344empty
21790.470.7624empty
31010.400.7615empty
4610.310.7517empty
5550.280.7416empty

Analyse

  • Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure

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