6jf0

Covalent labeling of hPPARg-LBD by turn-on fluorescent probe mediated by conjugate addition and cyclization

Method: X-RAY DIFFRACTION Dmax: 86.5 Å Quality: GOOD

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

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 232–505 Chain B; UniProt 232–505 Not recorded EB6 methyl (2~{S})-3-[4-[3-(4-methoxy-2-oxidanyl-phenyl)prop-2-ynoyloxy]phenyl]-2-[[2-(phenylcarbonyl)phenyl]amino]propanoate × 1 EBF 7-methoxychromen-2-one × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M Tris-HCl pH 7.4, 0.8 M sodium citrate Resolution 3.40 Å R-free 0.296

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 1
Chains and sequence ranges Author chain A; PDBConstruct 3–276; UniProt 232–505 Author chain B; PDBConstruct 3–276; UniProt 232–505

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 6jf0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6jf0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6jf0
Deposition date deposition_date2019-02-07
Structure title titleCovalent labeling of hPPARg-LBD by turn-on fluorescent probe mediated by conjugate addition and cyclization
Keywords keywordsRECEPTOR, covalent labeling, cysteine, turn-on fluorescent probe, TCC probe, NUCLEAR PROTEIN; NUCLEAR PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.80
Radius of gyration Rg (electron density) rg_electron24.71
Forward intensity I(0) i048898500.00
Molecular weight molecular_weight57382.0 kDa
Excluded volume excluded_volume73223 ų
Envelope volume envelope_volume87938 ų
Hydration-shell volume shell_volume29393 ų
Envelope diameter envelope_diameter87.4
Shell Rg shell_rg31.97
Envelope Rg envelope_rg24.91
Shape Rg shape_rg24.68
Total Rg total_rg25.68
Total atoms total_atoms4041
Residues n_residues503
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 dmax86.5
Rg (real space) rg_real25.74
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real4.8900e+07
I(0) uncertainty (real space) i0_real_error7.1770e+05
Rg (reciprocal space) rg_reciprocal25.76
I(0) (reciprocal space) i0_reciprocal48900000.0000
Solution quality estimate total_estimate0.8812
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.3
Skewness Skewness skewness0.298
Kurtosis Kurtosis kurtosis-0.320
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14140000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.834; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.949

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6jf0A00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id6jf0B00
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)