› 6ds6

X-ray diffraction
1.95Å resolution

Crystal structure of p300 ZZ domain in complex with histone H3 peptide

Released:
DOI: 10.2210/pdb6ds6/pdb
PDB entry 6ds6 coloured by chain, front view.
PDB entry 6ds6 coloured by chain, side view.
PDB entry 6ds6 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
The ZZ domain of p300 mediates specificity of the adjacent HAT domain for histone H3.
Zhang Y, Xue Y, Shi J, Ahn J, Mi W, Ali M, Wang X, Klein BJ, Wen H, Li W, Shi X, Kutateladze TG
Nat Struct Mol Biol 25 841-849 (2018)
PMID: 30150647

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170798 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase p300 Chain: A
Molecule details ›
Chain: A
Length: 57 amino acids
Theoretical weight: 6.85 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q09472 (Residues: 1661-1713; Coverage: 2%)
Gene names: EP300, P300
Sequence domains: Zinc finger, ZZ type
Structure domains: Wheat Germ Agglutinin (Isolectin 2); domain 1

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 4.2.2
Spacegroup: P43212
Unit cell:
a: 44.026Å b: 44.026Å c: 85.904Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.207 0.253
Expression system: Escherichia coli

Quick links

Citations

7 review citations

Histone acetyltransferases CBP/p300 in tumorigenesis and CBP/p300 inhibitors as promising novel anticancer agents.
Chen et al. (2022)
6 more

4 mentions without citation

The ZZ domain as a new epigenetic reader and a degradation signal sensor.
Zhang et al. (2019)
3 more