› 5x8x

X-ray diffraction
2.6Å resolution

Crystal Structure of the mutant Human ROR gamma Ligand Binding Domain With Compound A.

Released:
DOI: 10.2210/pdb5x8x/pdb
PDB entry 5x8x coloured by chain, front view.
PDB entry 5x8x coloured by chain, side view.
PDB entry 5x8x coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Ternary complex of human RORγ ligand-binding domain, inverse agonist and SMRT peptide shows a unique mechanism of corepressor recruitment.
Noguchi M, Nomura A, Murase K, Doi S, Yamaguchi K, Hirata K, Shiozaki M, Hirashima S, Kotoku M, Yamaguchi T, Katsuda Y, Steensma R, Li X, Tao H, Tse B, Fenn M, Babine R, Bradley E, Crowe P, Thacher S, Adachi T, Kamada M
Genes Cells 22 535-551 (2017)
PMID: 28493531

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-124206 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
RAR related orphan receptor C Chains: A, C, E, G
Molecule details ›
Chains: A, C, E, G
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 corepressor 2 Chains: B, D, F, H
Molecule details ›
Chains: B, D, F, H
Length: 22 amino acids
Theoretical weight: 2.6 KDa
Source organism: Homo sapiens
Expression system: synthetic construct
UniProt:
  • Canonical: Q9Y618 (Residues: 2335-2356; Coverage: 1%)
Gene names: CTG26, NCOR2

Ligands and Environments

1 bound ligand:
Ligand 82O 4 x 82O
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P21
Unit cell:
a: 79.3Å b: 72.6Å c: 99.32Å
α: 90° β: 89.98° γ: 90°
R-values:
R R work R free
0.2 0.199 0.233
Expression systems:
  • Escherichia coli
  • synthetic construct

Quick links

Citations

1 review citation

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

1 mention 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)