7cfo

Crystal structure of human RXRalpha ligand binding domain complexed with CBTF-EE.

Method: X-RAY DIFFRACTION Dmax: 90.2 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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 224–462 Chain B; UniProt 224–462 Chain C; UniProt 224–462 Chain D; UniProt 224–462 Fragment:ligand binding domain WZ6 1-[3-(2-ethoxyethoxy)-5,5,8,8-tetramethyl-6,7-dihydronaphthalen-2-yl]-2-(trifluoromethyl)benzimidazole-5-carboxylic acid × 3 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;295 K;5% [v/v] tacsimateTM [pH 7.0], 0.1 M HEPES [pH 7.0], and 10% [w/v] PEGMME5000 Resolution 2.15 Å R-free 0.266

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 5–243; UniProt 224–462 Author chain B; PDBConstruct 5–243; UniProt 224–462 Author chain C; PDBConstruct 5–243; UniProt 224–462 Author chain D; PDBConstruct 5–243; UniProt 224–462

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 7cfo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7cfo
Deposition date deposition_date2020-06-27
Structure title titleCrystal structure of human RXRalpha ligand binding domain complexed with CBTF-EE.
Keywords keywordsRetinoid X receptor alpha, antagonist, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.35
Radius of gyration Rg (electron density) rg_electron28.26
Forward intensity I(0) i0120782000.00
Molecular weight molecular_weight90791.0 kDa
Excluded volume excluded_volume115570 ų
Envelope volume envelope_volume141430 ų
Hydration-shell volume shell_volume40652 ų
Envelope diameter envelope_diameter93.9
Shell Rg shell_rg36.41
Envelope Rg envelope_rg27.82
Shape Rg shape_rg28.26
Total Rg total_rg29.06
Total atoms total_atoms6388
Residues n_residues792
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 dmax90.2
Rg (real space) rg_real29.22
Rg uncertainty (real space) rg_real_error0.53
I(0) (real space) i0_real1.2080e+08
I(0) uncertainty (real space) i0_real_error1.5140e+06
Rg (reciprocal space) rg_reciprocal29.28
I(0) (reciprocal space) i0_reciprocal120800000.0000
Solution quality estimate total_estimate0.9034
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.1
Skewness Skewness skewness0.205
Kurtosis Kurtosis kurtosis-0.469
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha31380000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd7cfob_
Class classa — All alpha proteins
Fold Fold folda.123 — Nuclear receptor ligand-binding domain
Superfamily Superfamily superfamilya.123.1 — Nuclear receptor ligand-binding domain
Family Family familya.123.1.1 — Nuclear receptor ligand-binding domain
Domain ID domain_idd7cfoc_
Class classa — All alpha proteins
Fold Fold folda.123 — Nuclear receptor ligand-binding domain
Superfamily Superfamily superfamilya.123.1 — Nuclear receptor ligand-binding domain
Family Family familya.123.1.1 — Nuclear receptor ligand-binding domain

8. Citations (1)

9. Files and Curves (10)