PDBe 5t0m

X-ray diffraction
1.9Å resolution

A histone H3K9M mutation traps histone methyltransferase Clr4 to prevent heterochromatin spreading

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-lysine N-methyltransferase EHMT2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 281 amino acids
Theoretical weight: 32.46 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: NEW Q96KQ7 (Residues: 913-1193; Coverage: 23%)
Gene names: BAT8, C6orf30, EHMT2, G9A, KMT1C, NG36
Sequence domains:
Structure domains: SET domain
Histone H3.1 Chains: C, P
Molecule details ›
Chains: C, P
Length: 15 amino acids
Theoretical weight: 1.55 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: NEW P68431 (Residues: 2-16; Coverage: 11%)
Gene names: H3FA, H3FB, H3FC, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3C, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments


Cofactor: Ligand SAM 2 x SAM

Cofactor: Ligand SAH 1 x SAH
1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P21
Unit cell:
a: 56.623Å b: 78.284Å c: 71.803Å
α: 90° β: 91.16° γ: 90°
R-values:
R R work R free
0.186 0.184 0.224
Expression systems:
  • Escherichia coli
  • Not provided