› 4n4h

X-ray diffraction
2.3Å resolution

Crystal structure of the Bromo-PWWP of the mouse zinc finger MYND-type containing 11 isoform alpha in complex with histone H3.1K36me3

Released:
DOI: 10.2210/pdb4n4h/pdb
PDB entry 4n4h coloured by chain, front view.
PDB entry 4n4h coloured by chain, side view.
PDB entry 4n4h coloured by chain, top view.
Source organisms:
Primary publication:
ZMYND11 links histone H3.3K36me3 to transcription elongation and tumour suppression.
Wen H, Li Y, Xi Y, Jiang S, Stratton S, Peng D, Tanaka K, Ren Y, Xia Z, Wu J, Li B, Barton MC, Li W, Li H, Shi X
Nature 508 263-8 (2014)
PMID: 24590075

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159425 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Zinc finger MYND domain-containing protein 11 Chain: A
Molecule details ›
Chain: A
Length: 252 amino acids
Theoretical weight: 29.5 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8R5C8 (Residues: 154-371; Coverage: 36%)
Gene name: Zmynd11
Sequence domains:
Structure domains:
Histone H3.1 Chain: B
Molecule details ›
Chain: B
Length: 22 amino acids
Theoretical weight: 2.4 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 22-43; Coverage: 16%)
Gene names: H3C1, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3FB, H3FC HIST1H3C, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand PO4 1 x PO4
Ligand PEG 1 x PEG
1 modified residue:
Ligand M3L 1 x M3L

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P43212
Unit cell:
a: 64.358Å b: 64.358Å c: 122.059Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.21 0.206 0.263
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

68 review citations

Histone exchange, chromatin structure and the regulation of transcription.
Venkatesh et al. (2015)
67 more

5 mentions without citation

Chemical and Biochemical Perspectives of Protein Lysine Methylation.
Luo M. (2018)
4 more