5ttf

X-ray diffraction
1.72Å resolution

Crystal structure of catalytic domain of G9a with MS012

Released:

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:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-188603 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase EHMT2 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 283 amino acids
Theoretical weight: 32.6 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P1
Unit cell:
a: 56.846Å b: 67.749Å c: 77.845Å
α: 92.09° β: 90.05° γ: 91.8°
R-values:
R R work R free
0.207 0.207 0.247
Expression system: Escherichia coli BL21(DE3)