› 1liq

Solution NMR

Non-native Solution Structure of a fragment of the CH1 domain of CBP

Released:
DOI: 10.2210/pdb1liq/pdb
PDB entry 1liq coloured by chain, ensemble of 20 models, front view.
PDB entry 1liq coloured by chain, ensemble of 20 models, side view.
PDB entry 1liq coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
A new zinc binding fold underlines the versatility of zinc binding modules in protein evolution.
Sharpe BK, Matthews JM, Kwan AH, Newton A, Gell DA, Crossley M, Mackay JP
Structure 10 639-48 (2002)
PMID: 12015147

Function and Biology Details

Reaction catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187751 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CREB-binding protein Chain: A
Molecule details ›
Chain: A
Length: 27 amino acids
Theoretical weight: 3.07 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: Q92793 (Residues: 376-402; Coverage: 1%)
Gene names: CBP, CREBBP
Sequence domains: TAZ zinc finger

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
Refinement method: distance geometry simulated annealing molecular dynamics
Expression system: Not provided

Quick links

Citations

4 review citations

Alpha-kinases: analysis of the family and comparison with conventional protein kinases.
Drennan et al. (2004)
3 more

3 mentions without citation

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