› 5th7

X-ray diffraction
1.95Å resolution

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)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192510 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-lysine methyltransferase KMT5A Chains: A, B
Molecule details ›
Chains: A, B
Length: 148 amino acids
Theoretical weight: 16.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9NQR1 (Residues: 234-380; Coverage: 37%)
Gene names: KMT5A, PRSET7, SET07, SET8, SETD8
Sequence domains: SET domain
Structure domains: SET domain

Ligands and Environments

3 bound ligands:
Ligand 7BY 2 x 7BY
Ligand UNX 21 x UNX
Ligand EDO 1 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2
Unit cell:
a: 83.15Å b: 31.64Å c: 114.89Å
α: 90° β: 105.23° γ: 90°
R-values:
R R work R free
0.192 0.189 0.237
Expression system: Escherichia coli BL21

Quick links

Citations

7 review citations

Epigenetics and beyond: targeting writers of protein lysine methylation to treat disease.
Bhat et al. (2021)
6 more

3 mentions without citation

Inhibitors of Protein Methyltransferases and Demethylases.
Kaniskan et al. (2018)
2 more