› 5i1q

X-ray diffraction
1.5Å resolution

Function and Biology Details

Reactions catalysed: 
Acetyl-CoA + [protein]-L-lysine = CoA + [protein]-N(6)-acetyl-L-lysine
ATP + a protein = ADP + a phosphoprotein
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149352 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription initiation factor TFIID subunit 1 Chain: A
Molecule details ›
Chain: A
Length: 144 amino acids
Theoretical weight: 16.58 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P21675 (Residues: 1518-1659; Coverage: 8%)
Gene names: BA2R, CCG1, CCGS, TAF1, TAF2A
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

1 bound ligand:
Ligand 67C 1 x 67C
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P212121
Unit cell:
a: 47.759Å b: 60.042Å c: 60.242Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.187 0.185 0.214
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Lysine Acetylation Goes Global: From Epigenetics to Metabolism and Therapeutics.
Ali et al. (2018)
8 more

7 mentions without citation

Structural features and inhibitors of bromodomains.
Meslamani et al. (2016)
6 more