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X-ray diffraction
1.75Å resolution

Crystal Structure of Human Histone-Lysine N-methyltransferase NSD1 SET domain in Complex with S-adenosyl-L-methionine

Released:
Source organism: Homo sapiens

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)
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase, H3 lysine-36 specific Chain: A
Molecule details ›
Chain: A
Length: 232 amino acids
Theoretical weight: 26.53 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q96L73 (Residues: 1852-2082; Coverage: 9%)
Gene names: ARA267, KMT3B, NSD1
Sequence domains:
Structure domains: SET domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U, BSRF BEAMLINE 1W2B
Spacegroup: P212121
Unit cell:
a: 65.875Å b: 67.751Å c: 69.086Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.165 0.164 0.186
Expression system: Escherichia coli