› 3t92

X-ray diffraction
1.5Å resolution

Crystal structure of the Taz2:C/EBPepsilon-TAD chimera protein

Released:
DOI: 10.2210/pdb3t92/pdb
PDB entry 3t92 coloured by chain, front view.
PDB entry 3t92 coloured by chain, side view.
PDB entry 3t92 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural insights into interactions of C/EBP transcriptional activators with the Taz2 domain of p300.
Bhaumik P, Davis J, Tropea JE, Cherry S, Johnson PF, Miller M
Acta Crystallogr D Biol Crystallogr 70 1914-21 (2014)
PMID: 25004968

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170792 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CCAAT/enhancer-binding protein epsilon; Histone acetyltransferase p300 Chain: A
Molecule details ›
Chain: A
Length: 121 amino acids
Theoretical weight: 13.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q09472 (Residues: 1723-1818; Coverage: 4%)
  • Canonical: Q15744 (Residues: 37-61; Coverage: 9%)
Gene names: CEBPE, EP300, P300
Sequence domains: TAZ zinc finger
Structure domains: TAZ domain

Ligands and Environments

4 bound ligands:
Ligand ZN 3 x ZN
Ligand TCE 1 x TCE
Ligand TAM 1 x TAM
Ligand ACN 1 x ACN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P65
Unit cell:
a: 47.86Å b: 47.86Å c: 104.13Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.18 0.178 0.228
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Natural Products with Antitumor Potential Targeting the MYB-C/EBPβ-p300 Transcription Module.
Schmidt et al. (2022)
10 other articles

7 mentions without citation

Protein lysine acetylation by p300/CBP.
Dancy et al. (2015)
6 more