4h12

X-ray diffraction
2.06Å resolution

The crystal structure of methyltransferase domain of human SET domain-containing protein 2 in complex with S-adenosyl-L-homocysteine

Released:

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)
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SETD2 Chain: A
Molecule details ›
Chain: A
Length: 278 amino acids
Theoretical weight: 31.96 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q9BYW2 (Residues: 1434-1711; Coverage: 11%)
Gene names: HIF1, HSPC069, HYPB, KIAA1732, KMT3A, SET2, SETD2
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: P212121
Unit cell:
a: 52.293Å b: 76.663Å c: 78.093Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.207 0.249
Expression system: Escherichia coli BL21