7bk4

Crystal structure of RXRalpha ligand binding domain in complex with a fragment of the TIF2 coactivator

Method: X-RAY DIFFRACTION Dmax: 72.8 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 223–462 Chain C; UniProt 223–462 Not recorded Nuclear receptor coactivator 2 × 2 (E7EWM1) LG2 6-[1-(3,5,5,8,8-PENTAMETHYL-5,6,7,8-TETRAHYDRONAPHTHALEN-2-YL)CYCLOPROPYL]PYRIDINE-3-CARBOXYLIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M Na Hepes, 0.2 M sodium acetate pH 7.5, 27% PEG 3350 Resolution 2.80 Å R-free 0.265

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 5–244; UniProt 223–462 Author chain C; PDBConstruct 5–244; UniProt 223–462

Nuclear receptor coactivator 2

OrganismNot specified

UniProt E7EWM1

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 686–713 Chain D; UniProt 686–713 Not recorded Retinoic acid receptor RXR-alpha × 2 (P19793) LG2 6-[1-(3,5,5,8,8-PENTAMETHYL-5,6,7,8-TETRAHYDRONAPHTHALEN-2-YL)CYCLOPROPYL]PYRIDINE-3-CARBOXYLIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M Na Hepes, 0.2 M sodium acetate pH 7.5, 27% PEG 3350 Resolution 2.80 Å R-free 0.265

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.

12 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name E7EWM1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–28; UniProt 686–713 Author chain D; PDBConstruct 1–28; UniProt 686–713

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 7bk4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7bk4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7bk4
Deposition date deposition_date2021-01-15
Structure title titleCrystal structure of RXRalpha ligand binding domain in complex with a fragment of the TIF2 coactivator
Keywords keywordsNuclear Receptor, Ligand binding domain, coactivator, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.70
Radius of gyration Rg (electron density) rg_electron22.39
Forward intensity I(0) i042118600.00
Molecular weight molecular_weight52511.0 kDa
Excluded volume excluded_volume66781 ų
Envelope volume envelope_volume78429 ų
Hydration-shell volume shell_volume28268 ų
Envelope diameter envelope_diameter72.8
Shell Rg shell_rg30.11
Envelope Rg envelope_rg22.55
Shape Rg shape_rg22.40
Total Rg total_rg23.28
Total atoms total_atoms3695
Residues n_residues462
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 dmax72.8
Rg (real space) rg_real23.53
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real4.2120e+07
I(0) uncertainty (real space) i0_real_error5.0450e+05
Rg (reciprocal space) rg_reciprocal23.57
I(0) (reciprocal space) i0_reciprocal42120000.0000
Solution quality estimate total_estimate0.9047
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.6
Skewness Skewness skewness0.108
Kurtosis Kurtosis kurtosis-0.517
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha9735000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.925; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)