1h3i

X-ray diffraction
2.1Å resolution

Crystal structure of the Histone Methyltransferase SET7/9

Released:

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)
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
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: 293 amino acids
Theoretical weight: 32.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8WTS6 (Residues: 52-344; Coverage: 80%)
Gene names: KIAA1717, KMT7, SET7, SET9, SETD7
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 66.09Å b: 82.83Å c: 116.15Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.21 0.255
Expression system: Escherichia coli