4ype

X-ray diffraction
2.2Å resolution

ASH1L SET domain H2193F mutant in complex with S-adenosyl methionine (SAM)

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)
Biological process:
  • not assigned
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase ASH1L Chains: A, B
Molecule details ›
Chains: A, B
Length: 226 amino acids
Theoretical weight: 26.03 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NR48 (Residues: 2074-2293; Coverage: 7%)
Gene names: ASH1L, KIAA1420, KMT2H
Sequence domains:
Structure domains: SET domain

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P3221
Unit cell:
a: 58.838Å b: 58.838Å c: 232.152Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.216 0.262
Expression system: Escherichia coli