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AlphaFold monomer V2.0 prediction for mycothiol acetyltransferase (Q5EDG0)

Analyse AlphaFold monomer V2.0 prediction for mycothiol acetyltransferase (Q5EDG0) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
Q5EDG0
Type
protein
Length
301 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x09DE4AAEB85d3D0679f6dB486Eff63b5c3a841aB
Molecule
Mycothiol acetyltransferase
UniProt
Q5EDG0
Pockets
3 · best druggability 0.79

Structure

1 distinct chain · 35% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AMycothiol acetyltransferaseprotein30135% helix, 29% strandQ5EDG0

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111110.790.8180empty
22570.720.8634empty
3530.360.7915empty

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