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AlphaFold monomer V2.0 prediction for bifunctional lysine-specific demethylase and histidyl-hydroxylase NO66 (B5DUH6)

Analyse AlphaFold monomer V2.0 prediction for bifunctional lysine-specific demethylase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

Accession
B5DUH6
Type
protein
Length
946 residues
Chains
1
Collection
MolNFT v1 / AlphaFold
Contract
0xBf7491af3407816DFa88a5EA4c82e8A2B1D721eD
Owner
0x2723cf191c24FC5306B779dD828bBaB5059845A2
Molecule
Bifunctional lysine-specific demethylase and histidyl- hydroxylase NO66
UniProt
B5DUH6
Pockets
7 · best druggability 0.76

Structure

1 distinct chain · 17% helix, 11% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABifunctional lysine-specific demethylase and histidyl- hydroxylase NO66protein94617% helix, 11% strandB5DUH6

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17880.760.8064empty
29300.760.7979empty
3530.670.9621empty
45730.660.7648empty
54770.580.7341empty

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