5ex0

X-ray diffraction
2.7Å resolution

Crystal structure of human SMYD3 in complex with a MAP3K2 peptide

Released:

Function and Biology Details

Reactions 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)
ATP + a protein = ADP + a phosphoprotein
Cellular component:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-190660 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-lysine N-methyltransferase SMYD3 Chain: A
Molecule details ›
Chain: A
Length: 431 amino acids
Theoretical weight: 49.54 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9H7B4 (Residues: 1-428; Coverage: 100%)
Gene names: SMYD3, ZMYND1, ZNFN3A1
Sequence domains:
Structure domains:
Mitogen-activated protein kinase kinase kinase 2 Chain: D
Molecule details ›
Chain: D
Length: 10 amino acids
Theoretical weight: 1.09 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q9Y2U5 (Residues: 256-265; Coverage: 2%)
Gene names: MAP3K2, MAPKKK2, MEKK2

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P212121
Unit cell:
a: 53.598Å b: 104.181Å c: 117.215Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.178 0.225
Expression systems:
  • Escherichia coli
  • Not provided