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Human lysine methyltransferase SMYD3 in complex with adohcy (form III)

Analyse Human lysine methyltransferase SMYD3 in complex with adohcy (form III) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OXG
Type
protein
Length
424 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Set and mynd domain-containing protein 3
EC
2.1.1.43
UniProt
Q9H7B4
Ligands
SAH, ZN
Pockets
3 · best druggability 0.78

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASet and mynd domain-containing protein 3 (EC 2.1.1.43)protein42449% helix, 12% strandQ9H7B4

Ligands and binding sites

  • SAH · S-adenosyl-L-homocysteine · ligand · chains A
  • ZN · Zinc ion · metal · 3 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110980.780.7995empty
22580.620.8138SAH
3740.370.7714empty

Compared structures

  • 3OXG · human lysine methyltransferase Smyd3 in complex with AdoHcy (Form III) · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9H7B4 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SMYD3 (Q9H7B4) · a predicted model of the same protein · chain A against A, TM-score 0.99

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