PDBe 5va6

X-ray diffraction
2.4Å resolution

CRYSTAL STRUCTURE OF ATXR5 IN COMPLEX WITH HISTONE H3.1 MONO-METHYLATED ON R26

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 229 amino acids
Theoretical weight: 26.22 KDa
Source organism: Ricinus communis
Expression system: Escherichia coli
UniProt:
  • Canonical: B9RU15 (Residues: 146-374; Coverage: 61%)
Gene names: ATXR5, RCOM_1460410
Histone H3.1 Chains: C, D
Molecule details ›
Chains: C, D
Length: 18 amino acids
Theoretical weight: 1.77 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 20-37; Coverage: 13%)
Gene names: H3FA, H3FB, H3FC, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3C, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
No bound ligands

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2
Unit cell:
a: 101.31Å b: 86.81Å c: 74.04Å
α: 90° β: 127.83° γ: 90°
R-values:
R R work R free
0.248 0.246 0.297
Expression systems:
  • Escherichia coli
  • Not provided