PDBe 3oxf

X-ray diffraction
2.82Å resolution

Human lysine methyltransferase Smyd3 in complex with AdoHcy (Form I)

Released:

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone]
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone-lysine N-methyltransferase SMYD3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 436 amino acids
Theoretical weight: 50.25 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H7B4 (Residues: 1-428; Coverage: 100%)
  • Best match: Q9H7B4-3 (Residues: 1-369)
Gene names: SMYD3, ZMYND1, ZNFN3A1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand SAH 2 x SAH
1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21
Unit cell:
a: 57.991Å b: 117.99Å c: 82.808Å
α: 90° β: 91.78° γ: 90°
R-values:
R R work R free
0.213 0.211 0.261
Expression system: Escherichia coli