3mqm

X-ray diffraction
2.54Å resolution

Crystal Structure of the Bromodomain of human ASH1L

Released:

Function and Biology Details

Reactions 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)
S-adenosyl-L-methionine + a [histone H3]-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(9)
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-192538 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase ASH1L Chains: A, B
Molecule details ›
Chains: A, B
Length: 126 amino acids
Theoretical weight: 14.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NR48 (Residues: 2438-2561; Coverage: 4%)
Gene names: ASH1L, KIAA1420, KMT2H
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: P65
Unit cell:
a: 69.59Å b: 69.59Å c: 151.34Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.207 0.204 0.259
Expression system: Escherichia coli