1k7l

The 2.5 Angstrom resolution crystal structure of the human PPARalpha ligand binding domain bound with GW409544 and a co-activator peptide.

Method: X-RAY DIFFRACTION Dmax: 119.2 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Peroxisome proliferator activated receptor alpha

Homo sapiens

UniProt Q07869

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 192–468 Fragment:ligand binding domain - residues 192 - 468 steroid receptor coactivator × 1 (O43792) 544 2-(1-METHYL-3-OXO-3-PHENYL-PROPYLAMINO)-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;PEG 3350, NaNO3, hexanediol, YCl3, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.50 Å R-free 0.284
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 192–468 Fragment:ligand binding domain - residues 192 - 468 steroid receptor coactivator × 1 (O43792) 544 2-(1-METHYL-3-OXO-3-PHENYL-PROPYLAMINO)-3-{4-[2-(5-METHYL-2-PHENYL-OXAZOL-4-YL)-ETHOXY]-PHENYL}-PROPIONIC ACID × 1 YT3 YTTRIUM (III) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;295 K;PEG 3350, NaNO3, hexanediol, YCl3, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.50 Å R-free 0.284
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 192–468 Fragment:ligand binding domain - residues 192 - 468 steroid receptor coactivator × 1 (O43792) 544 2-(1-METHYL-3-OXO-3-PHENYL-PROPYLAMINO)-3-{4-[2-(5-METHYL-2-PHENYL-OXAZOL-4-YL)-ETHOXY]-PHENYL}-PROPIONIC ACID × 1 YT3 YTTRIUM (III) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;295 K;PEG 3350, NaNO3, hexanediol, YCl3, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.50 Å R-free 0.284
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 192–468 Fragment:ligand binding domain - residues 192 - 468 steroid receptor coactivator × 1 (O43792) 544 2-(1-METHYL-3-OXO-3-PHENYL-PROPYLAMINO)-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;PEG 3350, NaNO3, hexanediol, YCl3, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.50 Å R-free 0.284

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.

78 other PDB entries and 103 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPAR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 12–288; UniProt 192–468 Author chain C; PDBConstruct 12–288; UniProt 192–468 Author chain E; PDBConstruct 12–288; UniProt 192–468 Author chain G; PDBConstruct 12–288; UniProt 192–468

steroid receptor coactivator

OrganismNot specified

UniProt O43792

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 680–700 Fragment:src-1 peptide Peroxisome proliferator activated receptor alpha × 1 (Q07869) 544 2-(1-METHYL-3-OXO-3-PHENYL-PROPYLAMINO)-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;PEG 3350, NaNO3, hexanediol, YCl3, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.50 Å R-free 0.284
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 680–700 Fragment:src-1 peptide Peroxisome proliferator activated receptor alpha × 1 (Q07869) 544 2-(1-METHYL-3-OXO-3-PHENYL-PROPYLAMINO)-3-{4-[2-(5-METHYL-2-PHENYL-OXAZOL-4-YL)-ETHOXY]-PHENYL}-PROPIONIC ACID × 1 YT3 YTTRIUM (III) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;295 K;PEG 3350, NaNO3, hexanediol, YCl3, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.50 Å R-free 0.284
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 680–700 Fragment:src-1 peptide Peroxisome proliferator activated receptor alpha × 1 (Q07869) 544 2-(1-METHYL-3-OXO-3-PHENYL-PROPYLAMINO)-3-{4-[2-(5-METHYL-2-PHENYL-OXAZOL-4-YL)-ETHOXY]-PHENYL}-PROPIONIC ACID × 1 YT3 YTTRIUM (III) ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;295 K;PEG 3350, NaNO3, hexanediol, YCl3, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.50 Å R-free 0.284
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 680–700 Fragment:src-1 peptide Peroxisome proliferator activated receptor alpha × 1 (Q07869) 544 2-(1-METHYL-3-OXO-3-PHENYL-PROPYLAMINO)-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;PEG 3350, NaNO3, hexanediol, YCl3, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K Resolution 2.50 Å R-free 0.284

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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O43792
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–21; UniProt 680–700 Author chain D; PDBConstruct 1–21; UniProt 680–700 Author chain F; PDBConstruct 1–21; UniProt 680–700 Author chain H; PDBConstruct 1–21; UniProt 680–700

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 1k7l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1k7l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1k7l
Deposition date deposition_date2001-10-19
Structure title titleThe 2.5 Angstrom resolution crystal structure of the human PPARalpha ligand binding domain bound with GW409544 and a co-activator peptide.
Keywords keywords;The 2.5 Angstrom resolution crystal structure of the human PPARalpha ligand binding domain bound with GW409544 and a coactivator peptide, TRANSCRIPTION ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier36.07
Radius of gyration Rg (electron density) rg_electron35.50
Forward intensity I(0) i0240885000.00
Molecular weight molecular_weight129350.0 kDa
Excluded volume excluded_volume163780 ų
Envelope volume envelope_volume213190 ų
Hydration-shell volume shell_volume50313 ų
Envelope diameter envelope_diameter122.6
Shell Rg shell_rg41.69
Envelope Rg envelope_rg34.91
Shape Rg shape_rg35.49
Total Rg total_rg35.99
Total atoms total_atoms9066
Residues n_residues1120
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 dmax119.2
Rg (real space) rg_real36.05
Rg uncertainty (real space) rg_real_error0.82
I(0) (real space) i0_real2.4090e+08
I(0) uncertainty (real space) i0_real_error3.5740e+06
Rg (reciprocal space) rg_reciprocal36.06
I(0) (reciprocal space) i0_reciprocal240900000.0000
Solution quality estimate total_estimate0.6726
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary43.3
Skewness Skewness skewness0.345
Kurtosis Kurtosis kurtosis-0.313
Angular range angular_range— – 0.2200 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha39290000.0000
Real-space data points n_real_points45
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 0.101; Positv: 1.000; Valcen: 0.999; Smooth: 0.860

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1k7la_
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_idd1k7lc_
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_idd1k7le_
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_idd1k7lg_
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 (4 domains)

Domain ID domain_id1k7lA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id1k7lC00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id1k7lE00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id1k7lG00
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)