PDBe 4n3w

X-ray diffraction
1.9Å resolution

Crystal Structure of the Bromodomain-PHD Finger Module of Human Transcriptional Co-Activator CBP in complex with Acetylated Histone 4 Peptide (H4K20ac).

Released:

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:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
CREB-binding protein Chain: A
Molecule details ›
Chain: A
Length: 237 amino acids
Theoretical weight: 27.95 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92793 (Residues: 1080-1316; Coverage: 10%)
Gene names: CBP, CREBBP
Sequence domains:
Structure domains:
Histone H4 Chain: C
Molecule details ›
Chain: C
Length: 15 amino acids
Theoretical weight: 1.8 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P62805 (Residues: 14-28; Coverage: 15%)
Gene names: H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4

Ligands and Environments

1 bound ligand:

1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X6A
Spacegroup: C2
Unit cell:
a: 92.46Å b: 59.312Å c: 53.444Å
α: 90° β: 102.96° γ: 90°
R-values:
R R work R free
0.256 0.233 0.286
Expression systems:
  • Escherichia coli
  • Not provided