4rfw

Crystal structure of human retinoid X Receptor alpha-ligand binding domain complex with 9cUAB70 and the coactivator peptide GRIP-1

Method: X-RAY DIFFRACTION Dmax: 56.2 Å Quality: REASONABLE

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 228–458 Fragment:ligand binding domain residues 228-458 Nuclear receptor coactivator 2 × 2 (Q15596) 3RB (2E,4E,6Z,8E)-3,7-dimethyl-8-(6,7,8,9-tetrahydro-5H-benzo[7]annulen-5-ylidene)octa-2,4,6-trienoic acid × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;5-12% PEG4000, 3-12 Glycerol, 0.1 Bis-Tris pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.40 Å R-free 0.261

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 1–231; UniProt 228–458

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 686–698 Fragment:coactivator peptide LXXLL motif 2, residues 686-698 Retinoic acid receptor RXR-alpha × 2 (P19793) 3RB (2E,4E,6Z,8E)-3,7-dimethyl-8-(6,7,8,9-tetrahydro-5H-benzo[7]annulen-5-ylidene)octa-2,4,6-trienoic acid × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;295 K;5-12% PEG4000, 3-12 Glycerol, 0.1 Bis-Tris pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.40 Å R-free 0.261

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 G; PDBConstruct 1–13; UniProt 686–698

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 4rfw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4rfw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4rfw
Deposition date deposition_date2014-09-28
Structure title titleCrystal structure of human retinoid X Receptor alpha-ligand binding domain complex with 9cUAB70 and the coactivator peptide GRIP-1
Keywords keywordsligand binding domain, cancer prevention, coactivator peptide, conformationally constrained retinoids, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.60
Radius of gyration Rg (electron density) rg_electron17.26
Forward intensity I(0) i011015600.00
Molecular weight molecular_weight25716.0 kDa
Excluded volume excluded_volume32705 ų
Envelope volume envelope_volume36866 ų
Hydration-shell volume shell_volume17781 ų
Envelope diameter envelope_diameter57.1
Shell Rg shell_rg23.52
Envelope Rg envelope_rg17.46
Shape Rg shape_rg17.27
Total Rg total_rg18.24
Total atoms total_atoms1810
Residues n_residues225
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 dmax56.2
Rg (real space) rg_real18.49
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real1.1020e+07
I(0) uncertainty (real space) i0_real_error1.3430e+05
Rg (reciprocal space) rg_reciprocal18.51
I(0) (reciprocal space) i0_reciprocal11020000.0000
Solution quality estimate total_estimate0.6876
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.1
Skewness Skewness skewness0.150
Kurtosis Kurtosis kurtosis-0.452
Angular range angular_range— – 0.4300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2295000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 0.995; Sysdev: 0.391; Positv: 1.000; Valcen: 0.989; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id4rfwA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor

8. Citations (1)

9. Files and Curves (10)