5bt3

X-ray diffraction
1.05Å resolution

Crystal structure of EP300 bromodomain in complex with SGC-CBP30 chemical probe

Released:
Source organism: Homo sapiens
Entry authors: Tallant C, Hay D, Krojer T, Nunez-Alonso G, Picaud S, Newman JA, Fedorov O, von Delft F, Arrowsmith CH, Edwards AM, Bountra C, Brennan PE, 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)
PDBe Complex ID:
PDB-CPX-170794 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histone acetyltransferase p300 Chain: A
Molecule details ›
Chain: A
Length: 116 amino acids
Theoretical weight: 13.83 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q09472 (Residues: 1048-1161; Coverage: 5%)
Gene names: EP300, P300
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P61
Unit cell:
a: 53.431Å b: 53.431Å c: 77.003Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.166 0.165 0.178
Expression system: Escherichia coli BL21(DE3)