5f59

X-ray diffraction
2.8Å resolution

The crystal structure of MLL3 SET domain

Released:

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-185520 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase 2C Chain: A
Molecule details ›
Chain: A
Length: 154 amino acids
Theoretical weight: 18 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8NEZ4 (Residues: 4757-4910; Coverage: 3%)
Gene names: HALR, KIAA1506, KMT2C, MLL3
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: SSRF BEAMLINE BL17U
Spacegroup: P4132
Unit cell:
a: 129.056Å b: 129.056Å c: 129.056Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.184 0.18 0.229
Expression system: Escherichia coli