› 1jjs

Solution NMR

NMR Structure of IBiD, A Domain of CBP/p300

Released:
DOI: 10.2210/pdb1jjs/pdb
PDB entry 1jjs coloured by chain, ensemble of 12 models, front view.
PDB entry 1jjs coloured by chain, ensemble of 12 models, side view.
PDB entry 1jjs coloured by chain, ensemble of 12 models, top view.
Source organism: Mus musculus
Primary publication:
A small domain of CBP/p300 binds diverse proteins: solution structure and functional studies.
Lin CH, Hare BJ, Wagner G, Harrison SC, Maniatis T, Fraenkel E
Mol Cell 8 581-90 (2001)
PMID: 11583620

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
Biological process:
Cellular component:
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: 50 amino acids
Theoretical weight: 5.58 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P45481 (Residues: 2067-2112; Coverage: 2%)
Gene names: Cbp, Crebbp
Sequence domains: Creb binding
Structure domains: Nuclear receptor coactivator, CREB-bp-like, interlocking domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: simulated annealing
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Intrinsically unstructured proteins and their functions.
Dyson et al. (2005)
9 more

6 mentions without citation

Modulation of epigenetic targets for anticancer therapy: clinicopathological relevance, structural data and drug discovery perspectives.
Andreoli et al. (2013)
5 more