› 5vb3

X-ray diffraction
1.95Å resolution

X-ray structure of nuclear receptor ROR-gammat Ligand Binding Domain + SRC2 peptide

Released:
DOI: 10.2210/pdb5vb3/pdb
PDB entry 5vb3 coloured by chain, front view.
PDB entry 5vb3 coloured by chain, side view.
PDB entry 5vb3 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural studies unravel the active conformation of apo RORγt nuclear receptor and a common inverse agonism of two diverse classes of RORγt inhibitors.
Li X, Anderson M, Collin D, Muegge I, Wan J, Brennan D, Kugler S, Terenzio D, Kennedy C, Lin S, Labadia ME, Cook B, Hughes R, Farrow NA
J Biol Chem 292 11618-11630 (2017)
PMID: 28546429

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-156322 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear receptor ROR-gamma; Nuclear receptor coactivator 2 Chain: A
Molecule details ›
Chain: A
Length: 280 amino acids
Theoretical weight: 32.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P51449 (Residues: 260-507; Coverage: 48%)
  • Canonical: Q15596 (Residues: 685-697; Coverage: 1%)
Gene names: BHLHE75, NCOA2, NR1F3, RORC, RORG, RZRG, SRC2, TIF2
Sequence domains: Ligand-binding domain of nuclear hormone receptor
Structure domains: Retinoid X Receptor

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P41212
Unit cell:
a: 61.272Å b: 61.272Å c: 154.226Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.196 0.23
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

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

5 mentions without citation

Structural studies unravel the active conformation of apo RORγt nuclear receptor and a common inverse agonism of two diverse classes of RORγt inhibitors.
Li et al. (2017)
4 more