3bo5

X-ray diffraction
1.59Å resolution

Crystal structure of methyltransferase domain of human Histone-lysine N-methyltransferase SETMAR

Released:
Source organism: Homo sapiens
Entry authors: Lunin VV, Wu H, Ren H, Dobrovetsky E, Weigelt J, Arrowsmith CH, Edwards AM, Bochkarev A, Min J, Plotnikov AN, Structural Genomics Consortium (SGC)

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)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SETMAR Chain: A
Molecule details ›
Chain: A
Length: 290 amino acids
Theoretical weight: 32.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q53H47 (Residues: 15-303; Coverage: 42%)
Gene name: SETMAR
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: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 41.396Å b: 67.827Å c: 44.637Å
α: 90° β: 105.93° γ: 90°
R-values:
R R work R free
0.157 0.155 0.199
Expression system: Escherichia coli