› 3vuz

X-ray diffraction
2.5Å resolution

Crystal structure of histone methyltransferase SET7/9 in complex with AAM-1

Released:
DOI: 10.2210/pdb3vuz/pdb
PDB entry 3vuz coloured by chain, front view.
PDB entry 3vuz coloured by chain, side view.
PDB entry 3vuz coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of histone methyltransferase SET7/9 in complexes with adenosylmethionine derivatives.
Niwa H, Handa N, Tomabechi Y, Honda K, Toyama M, Ohsawa N, Shirouzu M, Kagechika H, Hirano T, Umehara T, Yokoyama S
Acta Crystallogr D Biol Crystallogr 69 595-602 (2013)
PMID: 23519668

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 Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 29.08 KDa
Source organism: Homo sapiens
Expression system: CELL-FREE SYNTHESIS
UniProt:
  • Canonical: Q8WTS6 (Residues: 111-366; Coverage: 70%)
Gene names: KIAA1717, KMT7, SET7, SET9, SETD7
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand K15 1 x K15
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21212
Unit cell:
a: 101.807Å b: 39.223Å c: 67.045Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.186 0.183 0.247
Expression system: CELL-FREE SYNTHESIS

Quick links

Citations

4 review citations

Histone methyltransferases: novel targets for tumor and developmental defects.
Yi et al. (2015)
3 more

1 mention without citation

Deep Neural Network Classifier for Virtual Screening Inhibitors of (S)-Adenosyl-L-Methionine (SAM)-Dependent Methyltransferase Family.
Li et al. (2019)