› 3o35

X-ray diffraction
1.76Å resolution

Crystal structure of TRIM24 PHD-Bromo complexed with H3(23-31)K27ac peptide

Released:
DOI: 10.2210/pdb3o35/pdb
PDB entry 3o35 coloured by chain, front view.
PDB entry 3o35 coloured by chain, side view.
PDB entry 3o35 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
TRIM24 links a non-canonical histone signature to breast cancer.
Tsai WW, Wang Z, Yiu TT, Akdemir KC, Xia W, Winter S, Tsai CY, Shi X, Schwarzer D, Plunkett W, Aronow B, Gozani O, Fischle W, Hung MC, Patel DJ, Barton MC
Nature 468 927-32 (2010)
PMID: 21164480

Function and Biology Details

Reaction catalysed: 
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-127339 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Transcription intermediary factor 1-alpha Chains: A, B
Molecule details ›
Chains: A, B
Length: 184 amino acids
Theoretical weight: 21.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O15164 (Residues: 824-1006; Coverage: 17%)
Gene names: RNF82, TIF1, TIF1A, TRIM24
Sequence domains:
Structure domains:
Histone H3.1 Chains: D, E
Molecule details ›
Chains: D, E
Length: 9 amino acids
Theoretical weight: 943 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P68431 (Residues: 24-32; Coverage: 7%)
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

1 bound ligand:
Ligand ZN 4 x ZN
1 modified residue:
Ligand ALY 2 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 89.632Å b: 36.498Å c: 128.824Å
α: 90° β: 109.99° γ: 90°
R-values:
R R work R free
0.206 0.206 0.225
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided

Quick links

Citations

70 review citations

Histone methylation: a dynamic mark in health, disease and inheritance.
Greer et al. (2012)
69 more

4 mentions without citation

Acetylation- and Methylation-Related Epigenetic Proteins in the Context of Their Targets.
Javaid et al. (2017)
3 more