› 3b95

X-ray diffraction
2.99Å resolution

EuHMT1 (Glp) Ankyrin Repeat Domain (Structure 2)

Released:
DOI: 10.2210/pdb3b95/pdb
PDB entry 3b95 coloured by chain, front view.
PDB entry 3b95 coloured by chain, side view.
PDB entry 3b95 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The ankyrin repeats of G9a and GLP histone methyltransferases are mono- and dimethyllysine binding modules.
Collins RE, Northrop JP, Horton JR, Lee DY, Zhang X, Stallcup MR, Cheng X
Nat Struct Mol Biol 15 245-50 (2008)
PMID: 18264113

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
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159445 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
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: Ankyrin repeat-containing domain
Histone H3.1 Chain: P
Molecule details ›
Chain: P
Length: 15 amino acids
Theoretical weight: 1.59 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 2-16; Coverage: 11%)
Gene names: H3C1, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3FB, H3FC HIST1H3C, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments

1 bound ligand:
Ligand SO4 10 x SO4
1 modified residue:
Ligand MLY 1 x MLY

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: C2221
Unit cell:
a: 59.52Å b: 152.39Å c: 167.32Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.195 0.238
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

59 review citations

Histone methylation: a dynamic mark in health, disease and inheritance.
Greer et al. (2012)
58 more

17 mentions without citation

Perceiving the epigenetic landscape through histone readers.
Musselman et al. (2012)
16 more