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SET7/9-DNMT1 K142ME1 complex

Analyse SET7/9-DNMT1 K142ME1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OS5
Type
protein
Length
257 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Histone-lysine N-methyltransferase SETD7; DNMT1
EC
2.1.1.43
UniProt
Q8WTS6
Ligands
UNL, SAH
Pockets
1 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 11% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AHistone-lysine N-methyltransferase SETD7 (EC 2.1.1.43)protein24911% helix, 37% strandQ8WTS6
BDNMT1protein80% helix, 13% strand—

Ligands and binding sites

  • UNL · Unknown ligand · ligand · chains A
  • SAH · S-adenosyl-L-homocysteine · ligand · chains A, B
  • EDO · 1,2-ethanediol · additive · 5 copies · chains A, B
  • BME · Beta-mercaptoethanol · additive · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11400.440.7622SAH

Interfaces

1 interface between chains.

  • A–B · 720 Ų buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (methylation).

Compared structures

  • 3OS5 · SET7/9-Dnmt1 K142me1 complex · the same entry in another collection · chain A against A, TM-score 1.00
  • Q8WTS6 · AlphaFold monomer V2.0 prediction for histone-lysine N-methyltransferase SETD7 (Q8WTS6) · a predicted model of the same protein · chain A against A, TM-score 0.99

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