3vv0

X-ray diffraction
2Å resolution

Crystal structure of histone methyltransferase SET7/9 in complex with DAAM-3

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SETD7 Chain: A
Molecule details ›
Chain: A
Length: 263 amino acids
Theoretical weight: 29.08 KDa
Source organism: Homo sapiens
Expression system: CELL-FREE SYNTHESIS
UniProt:
  • Canonical: Q8WTS6 (Residues: 111-366; Coverage: 70%)
Gene names: KIAA1717, KMT7, SET7, SET9, SETD7
Sequence domains: SET domain
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL32XU
Spacegroup: P21212
Unit cell:
a: 101.836Å b: 39.126Å c: 67.322Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.232
Expression system: CELL-FREE SYNTHESIS