4z4p

X-ray diffraction
2.2Å resolution

Structure of the MLL4 SET Domain

Released:
Source organism: Homo sapiens
Primary publication:
Evolving Catalytic Properties of the MLL Family SET Domain.
Structure 23 1921-1933 (2015)
PMID: 26320581

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-127055 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase 2D Chain: A
Molecule details ›
Chain: A
Length: 166 amino acids
Theoretical weight: 19.7 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli #1/H766
UniProt:
  • Canonical: O14686 (Residues: 5379-5379, 5382-5536; Coverage: 3%)
Gene names: ALR, KMT2D, MLL2, MLL4
Sequence domains: SET domain
Structure domains: SET domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P21
Unit cell:
a: 38.299Å b: 40.692Å c: 50.965Å
α: 90° β: 109.78° γ: 90°
R-values:
R R work R free
0.196 0.193 0.242
Expression system: Escherichia coli #1/H766