PDBe 2rfi

X-ray diffraction
1.59Å resolution

Crystal structure of catalytic domain of human euchromatic histone methyltransferase 1 in complex with SAH and dimethylated H3K9 peptide

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

Assemblies composition:
hetero dimer (preferred)
hetero tetramer
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-lysine N-methyltransferase EHMT1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 285 amino acids
Theoretical weight: 32.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H9B1 (Residues: 982-1266; Coverage: 22%)
Gene names: EHMT1, EUHMTASE1, GLP, KIAA1876, KMT1D
Sequence domains:
Structure domains: SET domain
Histone H3 Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 11 amino acids
Theoretical weight: 1.16 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: P212121
Unit cell:
a: 84.593Å b: 85.627Å c: 95.67Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.193 0.22
Expression systems:
  • Escherichia coli
  • Not provided