6l37

X-ray structure of human PPARalpha ligand binding domain-GW9662-ciprofibrate co-crystals obtained by delipidation and co-crystallization

Method: X-RAY DIFFRACTION Dmax: 99.3 Å Quality: GOOD

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 200–468 Not recorded GW9 2-chloro-5-nitro-N-phenylbenzamide × 3 C5F 2-{4-[(1S)-2,2-dichlorocyclopropyl]phenoxy}-2-methylpropanoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;277 K;0.1 M Tris (pH 8.0), 25 %(w/v) PEG3350 Resolution 2.91 Å R-free 0.248
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 200–468 Not recorded GW9 2-chloro-5-nitro-N-phenylbenzamide × 3 C5F 2-{4-[(1S)-2,2-dichlorocyclopropyl]phenoxy}-2-methylpropanoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;277 K;0.1 M Tris (pH 8.0), 25 %(w/v) PEG3350 Resolution 2.91 Å R-free 0.248

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 105 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PPARA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 5–273; UniProt 200–468 Author chain B; PDBConstruct 5–273; UniProt 200–468

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 6l37

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6l37
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6l37
Deposition date deposition_date2019-10-09
Structure title titleX-ray structure of human PPARalpha ligand binding domain-GW9662-ciprofibrate co-crystals obtained by delipidation and co-crystallization
Keywords keywordsNuclear receptor, Protein-ligand complex, PPAR, Transcription; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.28
Radius of gyration Rg (electron density) rg_electron29.79
Forward intensity I(0) i059887000.00
Molecular weight molecular_weight62634.0 kDa
Excluded volume excluded_volume79184 ų
Envelope volume envelope_volume97892 ų
Hydration-shell volume shell_volume28518 ų
Envelope diameter envelope_diameter103.6
Shell Rg shell_rg35.43
Envelope Rg envelope_rg29.67
Shape Rg shape_rg29.78
Total Rg total_rg30.37
Total atoms total_atoms4471
Residues n_residues539
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 dmax99.3
Rg (real space) rg_real30.44
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real5.9890e+07
I(0) uncertainty (real space) i0_real_error1.0160e+06
Rg (reciprocal space) rg_reciprocal30.38
I(0) (reciprocal space) i0_reciprocal59880000.0000
Solution quality estimate total_estimate0.8617
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.7
Skewness Skewness skewness0.411
Kurtosis Kurtosis kurtosis-0.568
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21810000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.830; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.837; Smooth: 0.871

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6l37a1
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_idd6l37a2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6l37b_
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

8. Citations (1)

9. Files and Curves (10)