8pp0

Crystal structure of Retinoic Acid Receptor alpha (RXRA) in complexed with JP147

Method: X-RAY DIFFRACTION Dmax: 66.5 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 heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 223–462 Not recorded Nuclear receptor coactivator 2 × 1 (Q15596) 7QJ 3-[4-[2,3-dihydro-1H-inden-4-yl(methyl)amino]-6-(trifluoromethyl)pyrimidin-2-yl]oxypropanoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;23% PEG 3350, 0.1 M Ammonium actetate, 0.1 M tris pH 7.5 Resolution 1.90 Å R-free 0.223

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 3–242; UniProt 223–462

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 686–699 Not recorded Retinoic acid receptor RXR-alpha × 1 (P19793) 7QJ 3-[4-[2,3-dihydro-1H-inden-4-yl(methyl)amino]-6-(trifluoromethyl)pyrimidin-2-yl]oxypropanoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293.15 K;23% PEG 3350, 0.1 M Ammonium actetate, 0.1 M tris pH 7.5 Resolution 1.90 Å R-free 0.223

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 1–14; UniProt 686–699

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 8pp0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8pp0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8pp0
Deposition date deposition_date2023-07-05
Structure title titleCrystal structure of Retinoic Acid Receptor alpha (RXRA) in complexed with JP147
Keywords keywordsRXR alpha, inhibitor, Structural Genomics, Structural Genomics Consortium, SGC, DNA BINDING PROTEIN; DNA BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.48
Radius of gyration Rg (electron density) rg_electron17.22
Forward intensity I(0) i011286100.00
Molecular weight molecular_weight25816.0 kDa
Excluded volume excluded_volume32701 ų
Envelope volume envelope_volume37108 ų
Hydration-shell volume shell_volume17869 ų
Envelope diameter envelope_diameter56.9
Shell Rg shell_rg23.54
Envelope Rg envelope_rg17.46
Shape Rg shape_rg17.23
Total Rg total_rg18.19
Total atoms total_atoms1816
Residues n_residues227
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 dmax66.5
Rg (real space) rg_real18.38
Rg uncertainty (real space) rg_real_error0.50
I(0) (real space) i0_real1.1290e+07
I(0) uncertainty (real space) i0_real_error1.4640e+05
Rg (reciprocal space) rg_reciprocal18.39
I(0) (reciprocal space) i0_reciprocal11290000.0000
Solution quality estimate total_estimate0.7610
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.7
Skewness Skewness skewness0.148
Kurtosis Kurtosis kurtosis-0.468
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3249000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.639; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; 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)