› 4jlg

X-ray diffraction
1.9Å resolution

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-186700 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SETD7 Chains: A, B
Molecule details ›
Chains: A, B
Length: 264 amino acids
Theoretical weight: 29.68 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8WTS6 (Residues: 109-366; Coverage: 71%)
Gene names: KIAA1717, KMT7, SET7, SET9, SETD7
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand SAM 2 x SAM
Ligand 1L8 2 x 1L8
Ligand UNX 25 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P1
Unit cell:
a: 46.742Å b: 57.984Å c: 64.932Å
α: 83.33° β: 71.42° γ: 70.93°
R-values:
R R work R free
0.212 0.211 0.237
Expression system: Escherichia coli BL21

Quick links

Citations

32 review citations

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

10 mentions without citation

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