› 5ntq

X-ray diffraction
2.26Å resolution

Structural states of RORgt: X-ray elucidation of molecular mechanisms and binding interactions for natural and synthetic compounds

Released:
DOI: 10.2210/pdb5ntq/pdb
PDB entry 5ntq coloured by chain, front view.
PDB entry 5ntq coloured by chain, side view.
PDB entry 5ntq coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural States of RORγt: X-ray Elucidation of Molecular Mechanisms and Binding Interactions for Natural and Synthetic Compounds.
Kallen J, Izaac A, Be C, Arista L, Orain D, Kaupmann K, Guntermann C, Hoegenauer K, Hintermann S
ChemMedChem 12 1014-1021 (2017)
PMID: 28590087

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-156324 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear receptor ROR-gamma Chains: A, B
Molecule details ›
Chains: A, B
Length: 238 amino acids
Theoretical weight: 27.63 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P51449 (Residues: 263-499; Coverage: 46%)
Gene names: NR1F3, RORC, RORG, RZRG
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

1 bound ligand:
Ligand 444 2 x 444
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P61
Unit cell:
a: 99.748Å b: 99.748Å c: 124.392Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.239 0.238 0.257
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

(Inverse) Agonists of Retinoic Acid-Related Orphan Receptor γ: Regulation of Immune Responses, Inflammation, and Autoimmune Disease.
Jetten et al. (2020)
4 more

1 mention without citation

Statistical Analysis of Protein-Ligand Interaction Patterns in Nuclear Receptor RORγ.
Pham et al. (2022)