6kyp

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

Method: X-RAY DIFFRACTION Dmax: 97.9 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 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 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;277 K;0.1 M Tris (pH 8.5), 25 %(w/v) PEG3350 Resolution 2.86 Å R-free 0.244
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 E0O 2-(4-chloranylphenoxy)-2-methyl-propanoic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;277 K;0.1 M Tris (pH 8.5), 25 %(w/v) PEG3350 Resolution 2.86 Å R-free 0.244

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 6kyp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id6kyp
Deposition date deposition_date2019-09-19
Structure title titleX-ray structure of human PPARalpha ligand binding domain-GW9662-clofibric acid 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_guinier30.35
Radius of gyration Rg (electron density) rg_electron29.86
Forward intensity I(0) i059762500.00
Molecular weight molecular_weight62623.0 kDa
Excluded volume excluded_volume79170 ų
Envelope volume envelope_volume97395 ų
Hydration-shell volume shell_volume28298 ų
Envelope diameter envelope_diameter103.4
Shell Rg shell_rg35.53
Envelope Rg envelope_rg29.74
Shape Rg shape_rg29.85
Total Rg total_rg30.43
Total atoms total_atoms4455
Residues n_residues540
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 dmax97.9
Rg (real space) rg_real30.51
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real5.9760e+07
I(0) uncertainty (real space) i0_real_error9.4770e+05
Rg (reciprocal space) rg_reciprocal30.45
I(0) (reciprocal space) i0_reciprocal59760000.0000
Solution quality estimate total_estimate0.6763
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.4
Skewness Skewness skewness0.406
Kurtosis Kurtosis kurtosis-0.583
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha21240000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.851; Stabil: 1.000; Sysdev: 0.193; Positv: 1.000; Valcen: 0.854; Smooth: 0.801

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd6kypa1
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_idd6kypa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd6kypb1
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_idd6kypb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)