X-ray diffraction
1.5Å resolution

Crystal structure of a ternary complex of the human histone methyltransferase Pr-SET7 (also known as SET8)


Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + a [histone H4]-L-lysine(20) = S-adenosyl-L-homocysteine + a [histone H4]-N(6)-methyl-L-lysine(20)
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
N-lysine methyltransferase KMT5A Chains: A, E
Molecule details ›
Chains: A, E
Length: 161 amino acids
Theoretical weight: 18.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
  • Canonical: Q9NQR1 (Residues: 233-393; Coverage: 41%)
Gene names: KMT5A, PRSET7, SET07, SET8, SETD8
Sequence domains: SET domain
Structure domains: SET domain
SET and MYND domain-containing protein 5 Chains: B, F
Molecule details ›
Chains: B, F
Length: 10 amino acids
Theoretical weight: 1.37 KDa
Source organism: Homo sapiens
Expression system: Not provided
  • Canonical: Q6GMV2 (Residues: 364-365, 366-372; Coverage: 2%)
Gene names: RAI15, SMYD5

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P1
Unit cell:
a: 42.179Å b: 46.322Å c: 51.998Å
α: 64.74° β: 86.66° γ: 90.61°
R R work R free
0.188 0.187 0.206
Expression systems:
  • Escherichia coli
  • Not provided