› 2r3a

X-ray diffraction
2Å resolution

Methyltransferase domain of human suppressor of variegation 3-9 homolog 2

Released:
DOI: 10.2210/pdb2r3a/pdb
PDB entry 2r3a coloured by chain, front view.
PDB entry 2r3a coloured by chain, side view.
PDB entry 2r3a coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural biology of human H3K9 methyltransferases.
Wu H, Min J, Lunin VV, Antoshenko T, Dombrovski L, Zeng H, Allali-Hassani A, Campagna-Slater V, Vedadi M, Arrowsmith CH, Plotnikov AN, Schapira M
PLoS One 5 e8570 (2010)
PMID: 20084102

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(9)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-190623 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SUV39H2 Chain: A
Molecule details ›
Chain: A
Length: 300 amino acids
Theoretical weight: 33.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H5I1 (Residues: 112-410; Coverage: 73%)
Gene names: KMT1B, SUV39H2
Sequence domains:
Structure domains: SET domain

Ligands and Environments

3 bound ligands:
Ligand ZN 4 x ZN
Ligand SAM 1 x SAM
Ligand SER 1 x SER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 45.748Å b: 63.925Å c: 64.529Å
α: 90° β: 109.33° γ: 90°
R-values:
R R work R free
0.179 0.177 0.213
Expression system: Escherichia coli

Quick links

Citations

31 review citations

S-adenosyl-methionine-dependent methyltransferases: highly versatile enzymes in biocatalysis, biosynthesis and other biotechnological applications.
Struck et al. (2012)
30 more

22 mentions without citation

Histone lysine methylation dynamics: establishment, regulation, and biological impact.
Black et al. (2012)
21 more