1fm9

THE 2.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE HETERODIMER OF THE HUMAN RXRALPHA AND PPARGAMMA LIGAND BINDING DOMAINS RESPECTIVELY BOUND WITH 9-CIS RETINOIC ACID AND GI262570 AND CO-ACTIVATOR PEPTIDES.

Method: X-RAY DIFFRACTION Dmax: 81.9 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 225–462 Fragment:LIGAND BINDING DOMAIN - RESIDUES 225 - 462 PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA × 1 (P37231) STEROID RECEPTOR COACTIVATOR × 2 (O43793) 9CR (9cis)-retinoic acid × 1 570 2-(2-BENZOYL-PHENYLAMINO)-3-{4-[2-(5-METHYL-2-PHENYL-OXAZOL-4-YL)-ETHOXY]-PHENYL}-PROPIONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;295 K;17% PEG 4K, 200mM NaSCN, 8% Ethylene Glycol , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 22K Resolution 2.10 Å R-free 0.268

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 1–238; UniProt 225–462

PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA

Homo sapiens

UniProt P37231

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 D; UniProt 234–505 Fragment:LIGAND BINDING DOMAIN - RESIDUES 206 - 477 RETINOIC ACID RECEPTOR RXR-ALPHA × 1 (P19793) STEROID RECEPTOR COACTIVATOR × 2 (O43793) 9CR (9cis)-retinoic acid × 1 570 2-(2-BENZOYL-PHENYLAMINO)-3-{4-[2-(5-METHYL-2-PHENYL-OXAZOL-4-YL)-ETHOXY]-PHENYL}-PROPIONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;295 K;17% PEG 4K, 200mM NaSCN, 8% Ethylene Glycol , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 22K Resolution 2.10 Å R-free 0.268

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.

369 other PDB entries and 500 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPARG_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–272; UniProt 234–505

STEROID RECEPTOR COACTIVATOR

OrganismNot specified

UniProt O43793

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 675–701 Chain E; UniProt 675–701 Fragment:SRC-1 PEPTIDE RETINOIC ACID RECEPTOR RXR-ALPHA × 1 (P19793) PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA × 1 (P37231) 9CR (9cis)-retinoic acid × 1 570 2-(2-BENZOYL-PHENYLAMINO)-3-{4-[2-(5-METHYL-2-PHENYL-OXAZOL-4-YL)-ETHOXY]-PHENYL}-PROPIONIC ACID × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;295 K;17% PEG 4K, 200mM NaSCN, 8% Ethylene Glycol , pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 22K Resolution 2.10 Å R-free 0.268

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 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O43793
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–25; UniProt 675–701 Author chain E; PDBConstruct 1–25; UniProt 675–701

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 1fm9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1fm9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1fm9
Deposition date deposition_date2000-08-16
Structure title titleTHE 2.1 ANGSTROM RESOLUTION CRYSTAL STRUCTURE OF THE HETERODIMER OF THE HUMAN RXRALPHA AND PPARGAMMA LIGAND BINDING DOMAINS RESPECTIVELY BOUND WITH 9-CIS RETINOIC ACID AND GI262570 AND CO-ACTIVATOR PEPTIDES.
Keywords keywords;the heterodimer of the nuclear receptor ligand binding domains of RXRalpha and PPARgamma bound respectively with 9-cis Retinoic Acid and GI262570 and co-activator peptides, TRANSCRIPTION ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.19
Radius of gyration Rg (electron density) rg_electron23.77
Forward intensity I(0) i054799300.00
Molecular weight molecular_weight59776.0 kDa
Excluded volume excluded_volume75859 ų
Envelope volume envelope_volume90100 ų
Hydration-shell volume shell_volume30688 ų
Envelope diameter envelope_diameter87.2
Shell Rg shell_rg31.66
Envelope Rg envelope_rg24.10
Shape Rg shape_rg23.78
Total Rg total_rg24.65
Total atoms total_atoms4211
Residues n_residues530
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 dmax81.9
Rg (real space) rg_real25.09
Rg uncertainty (real space) rg_real_error0.42
I(0) (real space) i0_real5.4800e+07
I(0) uncertainty (real space) i0_real_error7.3510e+05
Rg (reciprocal space) rg_reciprocal25.12
I(0) (reciprocal space) i0_reciprocal54800000.0000
Solution quality estimate total_estimate0.8886
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.234
Kurtosis Kurtosis kurtosis-0.380
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14170000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.863; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.960

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1fm9a_
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_idd1fm9d_
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

CATH v4.4 (2 domains)

Domain ID domain_id1fm9A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id1fm9D00
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)