› 4nvq

X-ray diffraction
2.03Å resolution

Human G9a in Complex with Inhibitor A-366

Released:
DOI: 10.2210/pdb4nvq/pdb
PDB entry 4nvq coloured by chain, front view.
PDB entry 4nvq coloured by chain, side view.
PDB entry 4nvq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery and development of potent and selective inhibitors of histone methyltransferase g9a.
Sweis RF, Pliushchev M, Brown PJ, Guo J, Li F, Maag D, Petros AM, Soni NB, Tse C, Vedadi M, Michaelides MR, Chiang GG, Pappano WN
ACS Med Chem Lett 5 205-9 (2014)
PMID: 24900801

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a [histone H3]-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(9)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase EHMT2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 285 amino acids
Theoretical weight: 32.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96KQ7 (Residues: 913-1193; Coverage: 23%)
Gene names: BAT8, C6orf30, EHMT2, G9A, KMT1C, NG36
Sequence domains:
Structure domains: SET domain

Ligands and Environments

3 bound ligands:
Ligand 2OD 2 x 2OD
Ligand SAH 2 x SAH
Ligand ZN 8 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P21
Unit cell:
a: 56.14Å b: 78.25Å c: 71.44Å
α: 90° β: 92.61° γ: 90°
R-values:
R R work R free
0.203 0.202 0.239
Expression system: Escherichia coli

Quick links

Citations

36 review citations

The use of spirocyclic scaffolds in drug discovery.
Zheng et al. (2014)
35 more

6 mentions without citation

Inhibitors of Protein Methyltransferases and Demethylases.
Kaniskan et al. (2018)
5 more