PDBe 3o36

X-ray diffraction
1.7Å resolution

Crystal structure of TRIM24 PHD-Bromo complexed with H4(14-19)K16ac peptide

Released:

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

Structure analysis Details

Assembly composition:
hetero dimer (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: NEW O15164 (Residues: 824-1006; Coverage: 17%)
Gene names: RNF82, TIF1, TIF1A, TRIM24
Sequence domains:
Structure domains:
Histone H4 Chains: D, E
Molecule details ›
Chains: D, E
Length: 6 amino acids
Theoretical weight: 769 Da
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: NEW P62805 (Residues: 15-20; Coverage: 6%)
Gene names: H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 89.754Å b: 36.347Å c: 126.963Å
α: 90° β: 109.67° γ: 90°
R-values:
R R work R free
0.191 0.191 0.216
Expression systems:
  • Escherichia coli BL21(DE3)
  • Not provided