4rxj

X-ray diffraction
2.1Å resolution

crystal structure of WHSC1L1-PWWP2

Released:
Source organism: Homo sapiens
Primary publication:
Histone and DNA binding ability studies of the NSD subfamily of PWWP domains.
Biochem Biophys Res Commun 569 199-206 (2021)
PMID: 34271259

Function and Biology Details

Reactions catalysed:
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(27) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(27)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-189854 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase NSD3 Chain: A
Molecule details ›
Chain: A
Length: 113 amino acids
Theoretical weight: 13.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9BZ95 (Residues: 953-1064; Coverage: 8%)
Gene names: DC28, NSD3, WHSC1L1
Sequence domains: PWWP domain

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E
Spacegroup: C2221
Unit cell:
a: 79.357Å b: 99.476Å c: 41.552Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.23 0.272
Expression system: Escherichia coli