3dlm

X-ray diffraction
1.77Å resolution

Crystal structure of Tudor domain of human Histone-lysine N-methyltransferase SETDB1

Released:
Source organism: Homo sapiens
Entry authors: Amaya MF, Dombrovski L, Loppnau P, Bountra C, Weigelt J, Arrowsmith CH, Edwards AM, Bochkarev A, Min J, Wu H, Structural Genomics Consortium (SGC)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SETDB1 Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 24.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q15047 (Residues: 196-402; Coverage: 16%)
Gene names: ESET, KIAA0067, KMT1E, SETDB1
Sequence domains:
Structure domains: SH3 type barrels.

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ DW
Spacegroup: P212121
Unit cell:
a: 54.518Å b: 63.689Å c: 69.083Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.208 0.237
Expression system: Escherichia coli BL21