9qx6

Crystal structure of RXR alpha LBD bound to a synthetic agonist FN537 and a coactivator fragment

Method: X-RAY DIFFRACTION Dmax: 56.4 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

Retinoic acid receptor RXR-alpha

Homo sapiens

UniProt P19793

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 229–462 Not recorded Nuclear receptor coactivator 2 × 1 (Q15596) A1JAT (6R,6aR,7S,10R,10aS)-6-(3,5-bis(trifluoromethyl)phenyl)-5,6,6a,7,8,9,10,10a-octahydro-7,10-methanophenanthridine-3-carboxylic acid × 1 A1JHO 6S,6aS,7R,10S,10aR)-6-(3,5-bis(trifluoromethyl)phenyl)-5,6,6a,7,8,9,10,10a-octahydro-7,10-methanophenanthridine-3-carboxylic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;20% PEG3350, 0.2M calcium acetate Resolution 1.46 Å R-free 0.213

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

107 other PDB entries and 138 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RXRA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–235; UniProt 229–462

Nuclear receptor coactivator 2

OrganismNot specified

UniProt Q15596

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 687–696 Not recorded Retinoic acid receptor RXR-alpha × 1 (P19793) A1JAT (6R,6aR,7S,10R,10aS)-6-(3,5-bis(trifluoromethyl)phenyl)-5,6,6a,7,8,9,10,10a-octahydro-7,10-methanophenanthridine-3-carboxylic acid × 1 A1JHO 6S,6aS,7R,10S,10aR)-6-(3,5-bis(trifluoromethyl)phenyl)-5,6,6a,7,8,9,10,10a-octahydro-7,10-methanophenanthridine-3-carboxylic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;289 K;20% PEG3350, 0.2M calcium acetate Resolution 1.46 Å R-free 0.213

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

283 other PDB entries and 334 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCOA2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–10; UniProt 687–696

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9qx6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qx6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9qx6
Deposition date deposition_date2025-04-15
Structure title titleCrystal structure of RXR alpha LBD bound to a synthetic agonist FN537 and a coactivator fragment
Keywords keywordsRETINOIC ACID RECEPTOR RXR-ALPHA, Nuclear receptor, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier18.10
Radius of gyration Rg (electron density) rg_electron17.15
Forward intensity I(0) i021018000.00
Molecular weight molecular_weight23689.0 kDa
Excluded volume excluded_volume23051 ų
Envelope volume envelope_volume36155 ų
Hydration-shell volume shell_volume17572 ų
Envelope diameter envelope_diameter56.8
Shell Rg shell_rg23.39
Envelope Rg envelope_rg17.32
Shape Rg shape_rg17.14
Total Rg total_rg17.89
Total atoms total_atoms1796
Residues n_residues222
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax56.4
Rg (real space) rg_real17.99
Rg uncertainty (real space) rg_real_error0.28
I(0) (real space) i0_real2.1020e+07
I(0) uncertainty (real space) i0_real_error2.3310e+05
Rg (reciprocal space) rg_reciprocal18.00
I(0) (reciprocal space) i0_reciprocal21020000.0000
Solution quality estimate total_estimate0.9022
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.9
Skewness Skewness skewness0.177
Kurtosis Kurtosis kurtosis-0.453
Angular range angular_range— – 0.4400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4844000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.913; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)