3s7f

X-ray diffraction
2.85Å resolution

Structural Basis of Substrate Methylation and Inhibition of SMYD2

Released:

Function and Biology Details

Reaction catalysed:
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-164025 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
N-lysine methyltransferase SMYD2 Chain: A
Molecule details ›
Chain: A
Length: 433 amino acids
Theoretical weight: 49.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NRG4 (Residues: 1-433; Coverage: 100%)
Gene names: KMT3C, SMYD2
Sequence domains:
Structure domains:
p53 peptide Chain: I
Molecule details ›
Chain: I
Length: 13 amino acids
Theoretical weight: 1.38 KDa
Source organism: Homo sapiens
Expression system: Not provided

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: I4
Unit cell:
a: 156.413Å b: 156.413Å c: 52.895Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.172 0.201
Expression systems:
  • Escherichia coli
  • Not provided