› 5lsu

X-ray diffraction
2.14Å resolution

Structure of the Epigenetic Oncogene MMSET and inhibition by N-Alkyl Sinefungin Derivatives

Released:
DOI: 10.2210/pdb5lsu/pdb
PDB entry 5lsu coloured by chain, front view.
PDB entry 5lsu coloured by chain, side view.
PDB entry 5lsu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the Epigenetic Oncogene MMSET and Inhibition by N-Alkyl Sinefungin Derivatives.
Tisi D, Chiarparin E, Tamanini E, Pathuri P, Coyle JE, Hold A, Holding FP, Amin N, Martin AC, Rich SJ, Berdini V, Yon J, Acklam P, Burke R, Drouin L, Harmer JE, Jeganathan F, van Montfort RL, Newbatt Y, Tortorici M, Westlake M, Wood A, Hoelder S, Heightman TD
ACS Chem Biol 11 3093-3105 (2016)
PMID: 27571355

Function and Biology Details

Reaction catalysed: 
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(36) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(36)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132137 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase NSD2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 252 amino acids
Theoretical weight: 28.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O96028 (Residues: 973-1203; Coverage: 17%)
Gene names: KIAA1090, MMSET, NSD2, TRX5, WHSC1
Sequence domains:
Structure domains: SET domain

Ligands and Environments

2 bound ligands:
Ligand ZN 6 x ZN
Ligand SAM 2 x SAM
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P212121
Unit cell:
a: 94.583Å b: 63.114Å c: 81.094Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.171 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

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

6 mentions without citation

Chemical and Biochemical Perspectives of Protein Lysine Methylation.
Luo M. (2018)
5 more