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AlphaFold monomer V2.0 prediction for L-threonine 3-dehydrogenase (B7NES3)

Analyse AlphaFold monomer V2.0 prediction for L-threonine 3-dehydrogenase (B7NES3) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B7NES3
Type
protein
Length
341 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x0DCCBa59b2b48397411CAC3f11C2EbBaBBa4e79C
Molecule
L-threonine 3-dehydrogenase
UniProt
B7NES3
Pockets
1 · best druggability 0.66

Structure

1 distinct chain · 32% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AL-threonine 3-dehydrogenaseprotein34132% helix, 28% strandB7NES3

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15310.660.7745empty

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