5v9i

X-ray diffraction
1.74Å resolution

Crystal structure of catalytic domain of G9a with MS0105

Released:
Source organism: Homo sapiens
Entry authors: Dong A, Zeng H, Liu J, Xiong Y, Babault N, Jin J, Walker JR, Bountra C, Arrowsmith CH, Edwards AM, Wu H, Brown PJ, Structural Genomics Consortium (SGC)

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: P21
Unit cell:
a: 56.607Å b: 77.509Å c: 134.794Å
α: 90° β: 91.41° γ: 90°
R-values:
R R work R free
0.234 0.234 0.275
Expression system: Escherichia coli BL21(DE3)