› 3io2

X-ray diffraction
2.5Å resolution

Crystal structure of the Taz2 domain of p300

Released:
DOI: 10.2210/pdb3io2/pdb
PDB entry 3io2 coloured by chain, front view.
PDB entry 3io2 coloured by chain, side view.
PDB entry 3io2 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the Taz2 domain of p300: insights into ligand binding.
Miller M, Dauter Z, Cherry S, Tropea JE, Wlodawer A
Acta Crystallogr D Biol Crystallogr 65 1301-8 (2009)
PMID: 19966416

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-170794 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase p300 Chain: A
Molecule details ›
Chain: A
Length: 114 amino acids
Theoretical weight: 12.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q09472 (Residues: 1723-1836; Coverage: 5%)
Gene names: EP300, P300
Sequence domains: TAZ zinc finger
Structure domains: TAZ domain

Ligands and Environments

2 bound ligands:
Ligand ZN 3 x ZN
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: I4132
Unit cell:
a: 155.27Å b: 155.27Å c: 155.27Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.206 0.236
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Transcriptional/epigenetic regulator CBP/p300 in tumorigenesis: structural and functional versatility in target recognition.
Wang et al. (2013)
3 other articles

12 mentions without citation

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