3o33

X-ray diffraction
2Å resolution

Crystal structure of TRIM24 PHD-Bromo in the free state

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:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-127337 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription intermediary factor 1-alpha Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
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:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: P1
Unit cell:
a: 36.482Å b: 48.498Å c: 122.729Å
α: 86.45° β: 81.46° γ: 67.84°
R-values:
R R work R free
0.221 0.221 0.244
Expression system: Escherichia coli BL21(DE3)