4nqa

Crystal structure of liganded hRXR-alpha/hLXR-beta heterodimer on DNA

Method: X-RAY DIFFRACTION Dmax: 125.8 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 Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 98–462 Fragment:UNP residues 98-462 Liver X nuclear receptor beta × 1 (F1D8P7) Nuclear receptor coactivator 2 × 2 (Q15596) 5'-D(*TP*AP*AP*GP*GP*TP*CP*AP*CP*TP*TP*CP*AP*GP*GP*TP*CP*A)-3' × 1 5'-D(*TP*AP*TP*GP*AP*CP*CP*TP*GP*AP*AP*GP*TP*GP*AP*CP*CP*T)-3' × 1 9CR (9cis)-retinoic acid × 1 ZN ZINC ION × 4 965 [3-(3-{[2-chloro-3-(trifluoromethyl)benzyl](2,2-diphenylethyl)amino}propoxy)phenyl]acetic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;6% PEG8000, 18% isopropanol, 0.05 M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 3.10 Å R-free 0.218
2 Protein–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain H; UniProt 98–462 Fragment:UNP residues 98-462 Liver X nuclear receptor beta × 1 (F1D8P7) Nuclear receptor coactivator 2 × 2 (Q15596) 5'-D(*TP*AP*AP*GP*GP*TP*CP*AP*CP*TP*TP*CP*AP*GP*GP*TP*CP*A)-3' × 1 5'-D(*TP*AP*TP*GP*AP*CP*CP*TP*GP*AP*AP*GP*TP*GP*AP*CP*CP*T)-3' × 1 9CR (9cis)-retinoic acid × 1 ZN ZINC ION × 4 965 [3-(3-{[2-chloro-3-(trifluoromethyl)benzyl](2,2-diphenylethyl)amino}propoxy)phenyl]acetic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;6% PEG8000, 18% isopropanol, 0.05 M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 3.10 Å R-free 0.218

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 137 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 1–365; UniProt 98–462 Author chain H; PDBConstruct 1–365; UniProt 98–462

Liver X nuclear receptor beta

Homo sapiens

UniProt F1D8P7

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 Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 72–461 Fragment:UNP residues 72-461 Retinoic acid receptor RXR-alpha × 1 (P19793) Nuclear receptor coactivator 2 × 2 (Q15596) 5'-D(*TP*AP*AP*GP*GP*TP*CP*AP*CP*TP*TP*CP*AP*GP*GP*TP*CP*A)-3' × 1 5'-D(*TP*AP*TP*GP*AP*CP*CP*TP*GP*AP*AP*GP*TP*GP*AP*CP*CP*T)-3' × 1 9CR (9cis)-retinoic acid × 1 ZN ZINC ION × 4 965 [3-(3-{[2-chloro-3-(trifluoromethyl)benzyl](2,2-diphenylethyl)amino}propoxy)phenyl]acetic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;6% PEG8000, 18% isopropanol, 0.05 M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 3.10 Å R-free 0.218
2 Protein–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain I; UniProt 72–461 Fragment:UNP residues 72-461 Retinoic acid receptor RXR-alpha × 1 (P19793) Nuclear receptor coactivator 2 × 2 (Q15596) 5'-D(*TP*AP*AP*GP*GP*TP*CP*AP*CP*TP*TP*CP*AP*GP*GP*TP*CP*A)-3' × 1 5'-D(*TP*AP*TP*GP*AP*CP*CP*TP*GP*AP*AP*GP*TP*GP*AP*CP*CP*T)-3' × 1 9CR (9cis)-retinoic acid × 1 ZN ZINC ION × 4 965 [3-(3-{[2-chloro-3-(trifluoromethyl)benzyl](2,2-diphenylethyl)amino}propoxy)phenyl]acetic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;6% PEG8000, 18% isopropanol, 0.05 M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 3.10 Å R-free 0.218

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name F1D8P7_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–391; UniProt 72–461 Author chain I; PDBConstruct 2–391; UniProt 72–461

Nuclear receptor coactivator 2

Homo sapiens

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–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain C; UniProt 686–698 Chain D; UniProt 686–698 Fragment:peptide (UNP residues 686-698) Retinoic acid receptor RXR-alpha × 1 (P19793) Liver X nuclear receptor beta × 1 (F1D8P7) 5'-D(*TP*AP*AP*GP*GP*TP*CP*AP*CP*TP*TP*CP*AP*GP*GP*TP*CP*A)-3' × 1 5'-D(*TP*AP*TP*GP*AP*CP*CP*TP*GP*AP*AP*GP*TP*GP*AP*CP*CP*T)-3' × 1 9CR (9cis)-retinoic acid × 1 ZN ZINC ION × 4 965 [3-(3-{[2-chloro-3-(trifluoromethyl)benzyl](2,2-diphenylethyl)amino}propoxy)phenyl]acetic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;6% PEG8000, 18% isopropanol, 0.05 M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 3.10 Å R-free 0.218
2 Protein–DNA Heteromer Protein × 4 DNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain J; UniProt 686–698 Chain K; UniProt 686–698 Fragment:peptide (UNP residues 686-698) Retinoic acid receptor RXR-alpha × 1 (P19793) Liver X nuclear receptor beta × 1 (F1D8P7) 5'-D(*TP*AP*AP*GP*GP*TP*CP*AP*CP*TP*TP*CP*AP*GP*GP*TP*CP*A)-3' × 1 5'-D(*TP*AP*TP*GP*AP*CP*CP*TP*GP*AP*AP*GP*TP*GP*AP*CP*CP*T)-3' × 1 9CR (9cis)-retinoic acid × 1 ZN ZINC ION × 4 965 [3-(3-{[2-chloro-3-(trifluoromethyl)benzyl](2,2-diphenylethyl)amino}propoxy)phenyl]acetic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;295 K;6% PEG8000, 18% isopropanol, 0.05 M Tris, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 3.10 Å R-free 0.218

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 333 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NCOA2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–13; UniProt 686–698 Author chain D; PDBConstruct 1–13; UniProt 686–698 Author chain J; PDBConstruct 1–13; UniProt 686–698 Author chain K; 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 4nqa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id4nqa
Deposition date deposition_date2013-11-24
Structure title titleCrystal structure of liganded hRXR-alpha/hLXR-beta heterodimer on DNA
Keywords keywordsmulti-domain, RXR, LXR, DBD, LBD, ligand, zinc finger, TRANSCRIPTION REGULATOR-DNA complex; TRANSCRIPTION REGULATOR/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier41.20
Radius of gyration Rg (electron density) rg_electron40.17
Forward intensity I(0) i0625598000.00
Molecular weight molecular_weight186800.0 kDa
Excluded volume excluded_volume226520 ų
Envelope volume envelope_volume334930 ų
Hydration-shell volume shell_volume67748 ų
Envelope diameter envelope_diameter134.5
Shell Rg shell_rg47.32
Envelope Rg envelope_rg39.13
Shape Rg shape_rg40.15
Total Rg total_rg40.59
Total atoms total_atoms12978
Residues n_residues1507
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 dmax125.8
Rg (real space) rg_real40.95
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real6.2560e+08
I(0) uncertainty (real space) i0_real_error1.1700e+07
Rg (reciprocal space) rg_reciprocal41.20
I(0) (reciprocal space) i0_reciprocal625800000.0000
Solution quality estimate total_estimate0.8929
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.6
Skewness Skewness skewness-0.018
Kurtosis Kurtosis kurtosis-0.587
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha53370000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.880

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 8 domains

CATH v4.4 (8 domains)

Domain ID domain_id4nqaA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily10 — Erythroid Transcription Factor GATA-1, subunit A
Domain ID domain_id4nqaA02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id4nqaB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily10 — Erythroid Transcription Factor GATA-1, subunit A
Domain ID domain_id4nqaB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id4nqaH01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily10 — Erythroid Transcription Factor GATA-1, subunit A
Domain ID domain_id4nqaH02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id4nqaI01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology50 — Erythroid Transcription Factor GATA-1; Chain A
Homologous superfamily homologous superfamily10 — Erythroid Transcription Factor GATA-1, subunit A
Domain ID domain_id4nqaI02
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)