PDBe 3tg5

X-ray diffraction
2.3Å resolution

Structure of SMYD2 in complex with p53 and SAH

Released:
Source organism: Homo sapiens

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (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: 49.76 KDa
Source organism: Homo sapiens
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: Q9NRG4 (Residues: 1-433; Coverage: 100%)
Gene names: KMT3C, SMYD2
Sequence domains:
Structure domains:
Cellular tumor antigen p53 Chain: B
Molecule details ›
Chain: B
Length: 11 amino acids
Theoretical weight: 1.24 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P04637 (Residues: 365-375; Coverage: 3%)
Gene names: P53, TP53

Ligands and Environments


Cofactor: Ligand SAH 1 x SAH
2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 53.36Å b: 71.67Å c: 121.25Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.241 0.263
Expression systems:
  • Spodoptera frugiperda
  • Not provided