› 1tot

Solution NMR

ZZ Domain of CBP- a Novel Fold for a Protein Interaction Module

Released:
DOI: 10.2210/pdb1tot/pdb
PDB entry 1tot coloured by chain, ensemble of 20 models, front view.
PDB entry 1tot coloured by chain, ensemble of 20 models, side view.
PDB entry 1tot coloured by chain, ensemble of 20 models, top view.
Source organism: Mus musculus
Primary publication:
ZZ domain of CBP: an unusual zinc finger fold in a protein interaction module.
Legge GB, Martinez-Yamout MA, Hambly DM, Trinh T, Lee BM, Dyson HJ, Wright PE
J Mol Biol 343 1081-93 (2004)
PMID: 15476823

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 domain:

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 Chain: A
Molecule details ›
Chain: A
Length: 52 amino acids
Theoretical weight: 6.23 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P45481 (Residues: 1700-1751; Coverage: 2%)
Gene names: Cbp, Crebbp
Sequence domains: Zinc finger, ZZ type
Structure domains: Wheat Germ Agglutinin (Isolectin 2); domain 1

Ligands and Environments

1 bound ligand:
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics and simulated annealing
Expression system: Escherichia coli

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Citations

8 review citations

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

12 mentions without citation

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