PDBe 5v37

X-ray diffraction
1.42Å resolution

Crystal structure of SMYD3 with SAM and EPZ028862

Released:
Source organism: Homo sapiens
Entry author: Boriack-Sjodin PA

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 Chain: A
Molecule details ›
Chain: A
Length: 428 amino acids
Theoretical weight: 49.15 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:

Ligands and Environments


Cofactor: Ligand SAM 1 x SAM

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-D
Spacegroup: P212121
Unit cell:
a: 60.818Å b: 65.868Å c: 107.015Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.23 0.228 0.279
Expression system: Escherichia coli