PDBe 1peg

X-ray diffraction
2.59Å resolution

Structural basis for the product specificity of histone lysine methyltransferases

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

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone H3 Chains: P, Q
Molecule details ›
Chains: P, Q
Length: 15 amino acids
Theoretical weight: 1.57 KDa
Source organism: Kluyveromyces lactis NRRL Y-1140
Expression system: Not provided
UniProt:
  • Canonical: P61831 (Residues: 2-16; Coverage: 11%)
Gene names: HHT1, HHT2, KLLA0E08591g, KLLA0E17677g
Histone-lysine N-methyltransferase, H3 lysine-9 specific dim-5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 302 amino acids
Theoretical weight: 34.11 KDa
Source organism: Neurospora crassa
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8X225 (Residues: 30-331; Coverage: 91%)
Gene names: 29E8.110, NCU04402, dim-5
Sequence domains:
Structure domains: SET domain

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 68.26Å b: 94.17Å c: 114.69Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.32
Expression systems:
  • Not provided
  • Escherichia coli