› 4au7

X-ray diffraction
2.07Å resolution

The structure of the Suv4-20h2 ternary complex with histone H4

Released:
DOI: 10.2210/pdb4au7/pdb
PDB entry 4au7 coloured by chain, front view.
PDB entry 4au7 coloured by chain, side view.
PDB entry 4au7 coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
A novel route to product specificity in the Suv4-20 family of histone H4K20 methyltransferases.
Southall SM, Cronin NB, Wilson JR
Nucleic Acids Res 42 661-71 (2014)
PMID: 24049080

Function and Biology Details

Reactions catalysed: 
S-adenosyl-L-methionine + a [histone H4]-L-lysine(20) = S-adenosyl-L-homocysteine + a [histone H4]-N(6)-methyl-L-lysine(20)
S-adenosyl-L-methionine + a [histone H4]-N(6)-methyl-L-lysine(20) = S-adenosyl-L-homocysteine + a [histone H4]-N(6),N(6)-dimethyl-L-lysine(20)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
monomeric
Assembly name:
PDBe Complex ID:
PDB-CPX-158700 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Histone-lysine N-methyltransferase KMT5C Chains: A, B
Molecule details ›
Chains: A, B
Length: 247 amino acids
Theoretical weight: 28.16 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q6Q783 (Residues: 1-246; Coverage: 53%)
Gene names: Kmt5c, Suv420h2
Sequence domains: SET domain
Structure domains:
Histone H4 Chain: C
Molecule details ›
Chain: C
Length: 9 amino acids
Theoretical weight: 1.27 KDa
Source organism: Mus musculus
Expression system: Not provided
UniProt:
  • Canonical: P62806 (Residues: 18-26; Coverage: 9%)
Gene names: H4-12, H4-53, H4c1, H4c11, H4c12, H4c14, H4c16, H4c2, H4c3, H4c4, H4c6, H4c8, H4c9, H4f16, Hist1h4a, Hist1h4b, Hist1h4c, Hist1h4d, Hist1h4f, Hist1h4h, Hist1h4i, Hist1h4j, Hist1h4k, Hist1h4m, Hist2h4, Hist2h4a, Hist4h4

Ligands and Environments

3 bound ligands:
Ligand SAH 1 x SAH
Ligand ZN 3 x ZN
Ligand EDO 16 x EDO
1 modified residue:
Ligand MLY 1 x MLY

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 37.27Å b: 65.17Å c: 209.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.195 0.193 0.24
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

8 review citations

Writing, erasing and reading histone lysine methylations.
Hyun et al. (2017)
7 more

5 mentions without citation

Structure of the catalytic domain of EZH2 reveals conformational plasticity in cofactor and substrate binding sites and explains oncogenic mutations.
Wu et al. (2013)
4 more