› 5tuy

X-ray diffraction
2.6Å resolution

Structure of human G9a SET-domain (EHMT2) in complex with inhibitor MS0124

Released:
DOI: 10.2210/pdb5tuy/pdb
PDB entry 5tuy coloured by chain, front view.
PDB entry 5tuy coloured by chain, side view.
PDB entry 5tuy coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Discovery of Potent and Selective Inhibitors for G9a-Like Protein (GLP) Lysine Methyltransferase.
Xiong Y, Li F, Babault N, Dong A, Zeng H, Wu H, Chen X, Arrowsmith CH, Brown PJ, Liu J, Vedadi M, Jin J
J Med Chem 60 1876-1891 (2017)
PMID: 28135087

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: 268 amino acids
Theoretical weight: 30.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q96KQ7 (Residues: 921-1188; Coverage: 22%)
Gene names: BAT8, C6orf30, EHMT2, G9A, KMT1C, NG36
Sequence domains:
Structure domains: SET domain

Ligands and Environments

3 bound ligands:
Ligand ZN 8 x ZN
Ligand SAM 2 x SAM
Ligand 7L6 2 x 7L6
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 56.97Å b: 82.3Å c: 73.74Å
α: 90° β: 89.97° γ: 90°
R-values:
R R work R free
0.174 0.171 0.234
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

PROTACs: An Emerging Therapeutic Modality in Precision Medicine.
Nalawansha et al. (2020)
5 more

5 mentions without citation

Discovery of Potent and Selective Inhibitors for G9a-Like Protein (GLP) Lysine Methyltransferase.
Xiong et al. (2017)
4 more