4nyv

X-ray diffraction
1.83Å resolution

Crystal Structure of the Bromodomain of human CREBBP in complex with a quinazolin-one ligand

Released:
Source organism: Homo sapiens
Entry authors: Filippakopoulos P, Picaud S, Felletar I, Fedorov O, Martin S, Monteiro OP, von Delft F, Brennan P, Arrowsmith CH, Edwards AM, Bountra C, Knapp S, Structural Genomics Consortium (SGC)

Function and Biology Details

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

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 Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 119 amino acids
Theoretical weight: 14.22 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92793 (Residues: 1081-1197; Coverage: 5%)
Gene names: CBP, CREBBP
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: P1
Unit cell:
a: 36.15Å b: 55.68Å c: 69.08Å
α: 90.21° β: 104.03° γ: 108.61°
R-values:
R R work R free
0.195 0.192 0.251
Expression system: Escherichia coli BL21(DE3)