PDBe 3t92

X-ray diffraction
1.5Å resolution

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

Released:
Source organism: Homo sapiens
Primary publication:
Structural insights into interactions of C/EBP transcriptional activators with the Taz2 domain of p300.
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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (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: 13.42 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: NEW Q09472 (Residues: 1723-1818; Coverage: 4%)
  • Canonical: NEW Q15744 (Residues: 37-61; Coverage: 9%)
  • nullnull
Gene names: CEBPE, EP300, P300
Sequence domains: TAZ zinc finger
Structure domains: TAZ domain

Ligands and Environments


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)