3hna

X-ray diffraction
1.5Å resolution

Crystal structure of catalytic domain of human euchromatic histone methyltransferase 1 in complex with SAH and mono-Methylated H3K9 Peptide

Released:

Function and Biology Details

Biochemical function:
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: 287 amino acids
Theoretical weight: 32.97 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
Mono-Methylated H3K9 Peptide Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 11 amino acids
Theoretical weight: 1.26 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 83.526Å b: 83.372Å c: 95.13Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.166 0.193
Expression systems:
  • Escherichia coli
  • Not provided