› 6xcg

X-ray diffraction
1.64Å resolution

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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
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, C
Molecule details ›
Chains: A, B, C
Length: 141 amino acids
Theoretical weight: 16.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O96028 (Residues: 211-350; Coverage: 10%)
Gene names: KIAA1090, MMSET, NSD2, TRX5, WHSC1
Sequence domains: PWWP domain

Ligands and Environments

2 bound ligands:
Ligand V01 3 x V01
Ligand UNX 6 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: P1
Unit cell:
a: 49.566Å b: 49.978Å c: 51.179Å
α: 91.35° β: 91.88° γ: 118.27°
R-values:
R R work R free
0.179 0.178 0.222
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

Principles and functions of condensate modifying drugs.
Patel et al. (2022)
3 more

5 mentions without citation

Lysine methyltransferase inhibitors: where we are now.
Feoli et al. (2022)
4 more