9qj9

Crystal Structure of the Human Retinoid X Receptor DNA-Binding Domain Bound to Trim16 IR1 Response Element

Method: X-RAY DIFFRACTION Dmax: 58.4 Å Quality: GOOD

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–DNA Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 33–115 Chain B; UniProt 33–115 Not recorded ;DNA (5'-D(P*GP*GP*GP*GP*TP*CP*AP*TP*GP*AP*CP*CP*CP*T)-3') ; × 1 ;DNA (5'-D(P*GP*GP*GP*GP*TP*CP*AP*TP*GP*AP*CP*CP*CP*T)-3') ; × 1 ZN ZINC ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;290 K;20% PEG 1000, 0.2M MgCl2 0.1M NaCl, 0.05M Na cacodylate pH6.5 Resolution 3.50 Å R-free 0.335

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 P19793-2
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–87; UniProt 33–115 Author chain B; PDBConstruct 5–87; UniProt 33–115

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 9qj9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qj9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9qj9
Deposition date deposition_date2025-03-18
最后修订 last_revision2026-01-28
Structure title titleCrystal Structure of the Human Retinoid X Receptor DNA-Binding Domain Bound to Trim16 IR1 Response Element
Keywords keywordsDNA complex, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.55
Radius of gyration Rg (electron density) rg_electron18.30
Forward intensity I(0) i018609900.00
Molecular weight molecular_weight25032.0 kDa
Excluded volume excluded_volume27942 ų
Envelope volume envelope_volume35627 ų
Hydration-shell volume shell_volume16620 ų
Envelope diameter envelope_diameter59.1
Shell Rg shell_rg23.81
Envelope Rg envelope_rg18.23
Shape Rg shape_rg18.29
Total Rg total_rg18.94
Total atoms total_atoms1688
Residues n_residues168
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 dmax58.4
Rg (real space) rg_real18.47
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real1.8610e+07
I(0) uncertainty (real space) i0_real_error2.2140e+05
Rg (reciprocal space) rg_reciprocal18.49
I(0) (reciprocal space) i0_reciprocal18610000.0000
Solution quality estimate total_estimate0.8308
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.8
Skewness Skewness skewness0.192
Kurtosis Kurtosis kurtosis-0.514
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2241000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.932; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)