PDBe 5vac

X-ray diffraction
1.95Å resolution

Crystal Structure of ATXR5 SET domain in complex with K36me3 histone H3 peptide

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
Sequence domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Probable Histone-lysine N-methyltransferase ATXR5 Chain: A
Molecule details ›
Chain: A
Length: 229 amino acids
Theoretical weight: 26.2 KDa
Source organism: Ricinus communis
Expression system: Escherichia coli
UniProt:
  • Canonical: B9RU15 (Residues: 146-374; Coverage: 61%)
Gene names: ATXR5, RCOM_1460410
Histone H3.2 Chain: C
Molecule details ›
Chain: C
Length: 19 amino acids
Theoretical weight: 1.89 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q71DI3 (Residues: 19-37; Coverage: 14%)
Gene names: H3F2, H3FM, HIST2H3A, HIST2H3C, HIST2H3D

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: I222
Unit cell:
a: 74.548Å b: 81.353Å c: 88.503Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.189 0.228
Expression systems:
  • Escherichia coli
  • Not provided