PDBe 3b7b

X-ray diffraction
2.99Å resolution

EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 1)

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]. 
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase EHMT1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 237 amino acids
Theoretical weight: 26.18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H9B1 (Residues: 765-999; Coverage: 18%)
Gene names: EHMT1, EUHMTASE1, GLP, KIAA1876, KMT1D
Sequence domains: Ankyrin repeats (3 copies)
Structure domains: Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2221
Unit cell:
a: 59.79Å b: 151.26Å c: 167.85Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.205 0.261
Expression system: Escherichia coli