X-ray diffraction
1.85Å resolution

Structure of the transposase domain of human Histone-lysine N-methyltransferase SETMAR

Source organism: Homo sapiens
Entry authors: Amaya MF, Dombrovski L, Ni S, Bountra C, Weigelt J, Arrowsmith CH, Edwards AM, Botchkarev A, Min J, Plotnikov AN, Wu H, Structural Genomics Consortium (SGC)

Function and Biology Details

Reaction catalysed:
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(36) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(36)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-lysine N-methyltransferase SETMAR Chains: A, B
Molecule details ›
Chains: A, B
Length: 226 amino acids
Theoretical weight: 26.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q53H47 (Residues: 459-684; Coverage: 33%)
Gene name: SETMAR
Sequence domains: Transposase (partial DDE domain)
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H
LYFA Peptide Chain: C
Molecule details ›
Chain: C
Length: 4 amino acids
Theoretical weight: 513 Da
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E DW
Spacegroup: C2
Unit cell:
a: 158.826Å b: 46.521Å c: 61.748Å
α: 90° β: 92.04° γ: 90°
R R work R free
0.208 0.205 0.256
Expression systems:
  • Escherichia coli
  • Not provided