› 5u7g

X-ray diffraction
2.4Å resolution

Crystal Structure of the Catalytic Core of CBP

Released:
DOI: 10.2210/pdb5u7g/pdb
PDB entry 5u7g coloured by chain, front view.
PDB entry 5u7g coloured by chain, side view.
PDB entry 5u7g coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Role of the CBP catalytic core in intramolecular SUMOylation and control of histone H3 acetylation.
Park S, Stanfield RL, Martinez-Yamout MA, Dyson HJ, Wilson IA, Wright PE
Proc Natl Acad Sci U S A 114 E5335-E5342 (2017)
PMID: 28630323

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-155294 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone lysine acetyltransferase CREBBP Chains: A, B
Molecule details ›
Chains: A, B
Length: 621 amino acids
Theoretical weight: 72.64 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P45481 (Residues: 1079-1556; Coverage: 20%)
Gene names: Cbp, Crebbp
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 8 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: C2
Unit cell:
a: 214.173Å b: 87.17Å c: 114.977Å
α: 90° β: 109.68° γ: 90°
R-values:
R R work R free
0.256 0.254 0.283
Expression system: Escherichia coli

Quick links

Citations

8 review citations

CBP/p300: Critical Co-Activators for Nuclear Steroid Hormone Receptors and Emerging Therapeutic Targets in Prostate and Breast Cancers.
Waddell et al. (2021)
7 more

2 mentions without citation

The Biological Significance of Targeting Acetylation-Mediated Gene Regulation for Designing New Mechanistic Tools and Potential Therapeutics.
O'Garro et al. (2021)
1 more