› 5x8w

X-ray diffraction
2.3Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124205 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RAR related orphan receptor C Chain: A
Molecule details ›
Chain: A
Length: 258 amino acids
Theoretical weight: 29.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: G1RH57 (Residues: 240-497; Coverage: 52%)
Gene name: RORC
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor
Nuclear receptor coactivator 1 Chain: B
Molecule details ›
Chain: B
Length: 15 amino acids
Theoretical weight: 1.78 KDa
Source organism: Homo sapiens
Expression system: synthetic construct
UniProt:
  • Canonical: Q15788 (Residues: 686-700; Coverage: 1%)
Gene names: BHLHE74, NCOA1, SRC1

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-17A
Spacegroup: P41212
Unit cell:
a: 61.74Å b: 61.74Å c: 155.8Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.212 0.23
Expression systems:
  • Escherichia coli
  • synthetic construct

Quick links

Citations

1 review citation

RORγ Structural Plasticity and Druggability.
Huang et al. (2020)
4 other articles

2 mentions without citation

Ternary crystal structure of human RORγ ligand-binding-domain, an inhibitor and corepressor peptide provides a new insight into corepressor interaction.
Noguchi et al. (2018)
1 more