6by9

X-ray diffraction
2.3Å resolution

Crystal structure of EHMT1

Released:
Source organism: Homo sapiens
Entry authors: Dong A, Wei Y, Li A, Tempel W, Han S, Sunnerhagen M, Penn L, Bountra C, Arrowsmith CH, Edwards AM, Tong Y, 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:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-190698 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase EHMT1 Chain: A
Molecule details ›
Chain: A
Length: 328 amino acids
Theoretical weight: 35.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9H9B1 (Residues: 672-999; Coverage: 25%)
Gene names: EHMT1, EUHMTASE1, GLP, KIAA1876, KMT1D
Sequence domains: Ankyrin repeats (3 copies)

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P3121
Unit cell:
a: 53.681Å b: 53.681Å c: 204.45Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.217 0.238
Expression system: Escherichia coli BL21