6yik

X-ray diffraction
1.7Å resolution

Crystal structure of the CREBBP bromodomain in complex with a tetrahydroquinoxaline ligand

Released:
Source organism: Homo sapiens
Entry authors: Picaud S, Brand M, Tobias K, von Delft F, Arrowsmith CH, Edwards AM, Bountra C, Conway S, Filippakopoulos P

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CREB-binding protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
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

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 80.23Å b: 43.907Å c: 88.27Å
α: 90° β: 110.06° γ: 90°
R-values:
R R work R free
0.157 0.156 0.184
Expression system: Escherichia coli BL21(DE3)