› 1eqf

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF THE DOUBLE BROMODOMAIN MODULE FROM HUMAN TAFII250

Released:
DOI: 10.2210/pdb1eqf/pdb
PDB entry 1eqf coloured by chain, front view.
PDB entry 1eqf coloured by chain, side view.
PDB entry 1eqf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure and function of a human TAFII250 double bromodomain module.
Jacobson RH, Ladurner AG, King DS, Tjian R
Science 288 1422-5 (2000)
PMID: 10827952

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 domain:

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: 280 amino acids
Theoretical weight: 32.71 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21675 (Residues: 1380-1659; Coverage: 15%)
Gene names: BA2R, CCG1, CCGS, TAF1, TAF2A
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

1 bound ligand:
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 48.1Å b: 58.1Å c: 101.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.246 0.218 0.246
Expression system: Escherichia coli

Quick links

Citations

173 review citations

The diverse functions of histone lysine methylation.
Martin et al. (2005)
172 more

21 mentions without citation

How chromatin-binding modules interpret histone modifications: lessons from professional pocket pickers.
Taverna et al. (2007)
20 more