2yyn

X-ray diffraction
2.5Å resolution

Crystal structure of human bromodomain protein

Released:
Source organism: Homo sapiens
Entry authors: Kishishita S, Uchikubo-Kamo T, Murayama K, Terada T, Shirouzu M, Yokoyama S, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-127340 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Transcription intermediary factor 1-alpha Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 135 amino acids
Theoretical weight: 15.49 KDa
Source organism: Homo sapiens
Expression system: cell-free protein synthesis
UniProt:
  • Canonical: O15164 (Residues: 891-1012; Coverage: 12%)
Gene names: RNF82, TIF1, TIF1A, TRIM24
Sequence domains: Bromodomain
Structure domains: Bromodomain-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P212121
Unit cell:
a: 75.855Å b: 76.16Å c: 107.599Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.239 0.239 0.285
Expression system: cell-free protein synthesis