2acl

Liver X-Receptor alpha Ligand Binding Domain with SB313987

Method: X-RAY DIFFRACTION Dmax: 146.3 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 225–462 Not recorded Oxysterols receptor LXR-alpha × 1 (Q9Z0Y9) REA RETINOIC ACID × 1 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 225–462 Not recorded Oxysterols receptor LXR-alpha × 1 (Q9Z0Y9) REA RETINOIC ACID × 1 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 225–462 Not recorded Oxysterols receptor LXR-alpha × 1 (Q9Z0Y9) REA RETINOIC ACID × 1 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 225–462 Not recorded Oxysterols receptor LXR-alpha × 1 (Q9Z0Y9) REA RETINOIC ACID × 1 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280
5 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 225–462 Chain G; UniProt 225–462 Not recorded Oxysterols receptor LXR-alpha × 2 (Q9Z0Y9) REA RETINOIC ACID × 2 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280
6 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 225–462 Chain E; UniProt 225–462 Not recorded Oxysterols receptor LXR-alpha × 2 (Q9Z0Y9) REA RETINOIC ACID × 2 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280

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 133 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 1–238; UniProt 225–462 Author chain C; PDBConstruct 1–238; UniProt 225–462 Author chain E; PDBConstruct 1–238; UniProt 225–462 Author chain G; PDBConstruct 1–238; UniProt 225–462

Oxysterols receptor LXR-alpha

Mus musculus

UniProt Q9Z0Y9

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 203–445 Not recorded Retinoic acid receptor RXR-alpha × 1 (P19793) REA RETINOIC ACID × 1 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 203–445 Not recorded Retinoic acid receptor RXR-alpha × 1 (P19793) REA RETINOIC ACID × 1 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 203–445 Not recorded Retinoic acid receptor RXR-alpha × 1 (P19793) REA RETINOIC ACID × 1 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 203–445 Not recorded Retinoic acid receptor RXR-alpha × 1 (P19793) REA RETINOIC ACID × 1 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280
5 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 203–445 Chain H; UniProt 203–445 Not recorded Retinoic acid receptor RXR-alpha × 2 (P19793) REA RETINOIC ACID × 2 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280
6 Protein heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 203–445 Chain F; UniProt 203–445 Not recorded Retinoic acid receptor RXR-alpha × 2 (P19793) REA RETINOIC ACID × 2 L05 1-BENZYL-3-(4-METHOXYPHENYLAMINO)-4-PHENYLPYRROLE-2,5-DIONE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;298 K;PEG3350, Ammonium Acetate, BisTris, Dtt, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 2.80 Å R-free 0.280

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.

1 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NR1H3_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 2–244; UniProt 203–445 Author chain D; PDBConstruct 2–244; UniProt 203–445 Author chain F; PDBConstruct 2–244; UniProt 203–445 Author chain H; PDBConstruct 2–244; UniProt 203–445

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 2acl

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2acl
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2acl
Deposition date deposition_date2005-07-19
Structure title titleLiver X-Receptor alpha Ligand Binding Domain with SB313987
Keywords keywordsnuclear hormone receptor ligand binding domain transcription factor three layered a-helix fold, TRANSCRIPTION; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier44.28
Radius of gyration Rg (electron density) rg_electron43.97
Forward intensity I(0) i0607058000.00
Molecular weight molecular_weight210290.0 kDa
Excluded volume excluded_volume266190 ų
Envelope volume envelope_volume351140 ų
Hydration-shell volume shell_volume66501 ų
Envelope diameter envelope_diameter149.5
Shell Rg shell_rg48.97
Envelope Rg envelope_rg43.01
Shape Rg shape_rg43.94
Total Rg total_rg44.30
Total atoms total_atoms14822
Residues n_residues1827
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 dmax146.3
Rg (real space) rg_real44.32
Rg uncertainty (real space) rg_real_error1.21
I(0) (real space) i0_real6.0710e+08
I(0) uncertainty (real space) i0_real_error1.1890e+07
Rg (reciprocal space) rg_reciprocal44.28
I(0) (reciprocal space) i0_reciprocal607000000.0000
Solution quality estimate total_estimate0.8218
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.8
Skewness Skewness skewness0.326
Kurtosis Kurtosis kurtosis-0.551
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha92030000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 20 domains

SCOP 2.08 (12 domains)

Domain ID domain_idd2acla_
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_idd2aclb1
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_idd2aclb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2aclc_
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_idd2acld2
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_idd2acld3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2acle_
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_idd2aclf2
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_idd2aclf3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd2aclg_
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_idd2aclh2
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_idd2aclh3
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (8 domains)

Domain ID domain_id2aclA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id2aclB00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id2aclC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id2aclD00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id2aclE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id2aclF00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id2aclG00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id2aclH00
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)