PDBe 1o9s

X-ray diffraction
1.75Å resolution

Crystal structure of a ternary complex of the human histone methyltransferase SET7/9

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-lysine N-methyltransferase SETD7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 259 amino acids
Theoretical weight: 28.91 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WTS6 (Residues: 108-366; Coverage: 71%)
Gene names: KIAA1717, KMT7, SET7, SET9, SETD7
Sequence domains: SET domain
Structure domains:
Histone H3.1 Chains: K, L
Molecule details ›
Chains: K, L
Length: 10 amino acids
Theoretical weight: 1.24 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 2-11; Coverage: 7%)
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: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 52.69Å b: 75.438Å c: 69.099Å
α: 90° β: 94.16° γ: 90°
R-values:
R R work R free
0.206 0.205 0.222
Expression systems:
  • Escherichia coli
  • Not provided