X-ray diffraction
1.83Å resolution

Crystal structure of TRIM24 PHD-bromodomain complexed with N-{1,3-dimethyl-6-[3-(2-methylpropoxy)phenoxy]-2-oxo-2,3-dihydro-1H-1,3-benzodiazol-5-yl}-1,2-dimethyl-1H-imidazole-4-sulfonamide (7g)


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:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Transcription intermediary factor 1-alpha Chain: A
Molecule details ›
Chain: A
Length: 184 amino acids
Theoretical weight: 21.32 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
  • Canonical: O15164 (Residues: 824-1006; Coverage: 17%)
Gene names: RNF82, TIF1, TIF1A, TRIM24
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.3.1
Spacegroup: C2
Unit cell:
a: 90.735Å b: 36.238Å c: 65.935Å
α: 90° β: 111.56° γ: 90°
R R work R free
0.17 0.167 0.231
Expression system: Escherichia coli BL21(DE3)