7prv

The glucocorticoid receptor in complex with fluticasone furoate, a PGC1a coactivator fragment and sgk 23bp

Method: X-RAY DIFFRACTION Dmax: 94.2 Å Quality: EXCELLENT

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

Glucocorticoid receptor

Homo sapiens

UniProt P04150

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–DNA Heteromer Protein × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain A; UniProt 385–777 Chain B; UniProt 385–777 Mutation:S404A, N517D, V571M, F602S, C638D ;DNA (5'-D(*TP*CP*GP*AP*CP*GP*GP*AP*CP*AP*AP*AP*AP*TP*GP*TP*TP*CP*TP*GP*TP*A)-3') ; × 1 ;DNA (5'-D(*TP*AP*CP*AP*GP*AP*AP*CP*AP*TP*TP*TP*TP*GP*TP*CP*CP*GP*TP*CP*GP*A)-3') ; × 1 Peroxisome proliferator-activated receptor gamma coactivator 1-alpha × 1 (Q9UBK2) ZN ZINC ION × 4 EDO 1,2-ETHANEDIOL × 3 GW6 (6alpha,11alpha,14beta,16alpha,17alpha)-6,9-difluoro-17-{[(fluoromethyl)sulfanyl]carbonyl}-11-hydroxy-16-methyl-3-oxoan drosta-1,4-dien-17-yl furan-2-carboxylate × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;8 % PEG3350, 0.3 M 1,6-hexanediol, 0.1 M guanidine hydrochloride, 8 % 2,2,2-trifluoroethanol, 0.1 M Bis Tris Propane pH 6.5 Resolution 2.70 Å R-free 0.253

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.

54 other PDB entries and 79 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–393; UniProt 385–777 Author chain B; PDBConstruct 1–393; UniProt 385–777

Peroxisome proliferator-activated receptor gamma coactivator 1-alpha

OrganismNot specified

UniProt Q9UBK2

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–DNA Heteromer Protein × 3 DNA 2 PDB declaration: pentameric(5) Consistent with all polymer counts Chain F; UniProt 134–154 Not recorded Glucocorticoid receptor × 2 (P04150) ;DNA (5'-D(*TP*CP*GP*AP*CP*GP*GP*AP*CP*AP*AP*AP*AP*TP*GP*TP*TP*CP*TP*GP*TP*A)-3') ; × 1 ;DNA (5'-D(*TP*AP*CP*AP*GP*AP*AP*CP*AP*TP*TP*TP*TP*GP*TP*CP*CP*GP*TP*CP*GP*A)-3') ; × 1 ZN ZINC ION × 4 EDO 1,2-ETHANEDIOL × 3 GW6 (6alpha,11alpha,14beta,16alpha,17alpha)-6,9-difluoro-17-{[(fluoromethyl)sulfanyl]carbonyl}-11-hydroxy-16-methyl-3-oxoan drosta-1,4-dien-17-yl furan-2-carboxylate × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;8 % PEG3350, 0.3 M 1,6-hexanediol, 0.1 M guanidine hydrochloride, 8 % 2,2,2-trifluoroethanol, 0.1 M Bis Tris Propane pH 6.5 Resolution 2.70 Å R-free 0.253

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.

39 other PDB entries and 44 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRGC1_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain F; PDBConstruct 1–21; UniProt 134–154

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 7prv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7prv
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7prv
Deposition date deposition_date2021-09-22
Structure title titleThe glucocorticoid receptor in complex with fluticasone furoate, a PGC1a coactivator fragment and sgk 23bp
Keywords keywordsnuclear receptor, ligand-activated transcription factor, multi-domain, complex, agonist, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.86
Radius of gyration Rg (electron density) rg_electron29.57
Forward intensity I(0) i0152861000.00
Molecular weight molecular_weight90344.0 kDa
Excluded volume excluded_volume109690 ų
Envelope volume envelope_volume140740 ų
Hydration-shell volume shell_volume39142 ų
Envelope diameter envelope_diameter97.1
Shell Rg shell_rg37.20
Envelope Rg envelope_rg29.54
Shape Rg shape_rg29.54
Total Rg total_rg30.30
Total atoms total_atoms6248
Residues n_residues698
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 dmax94.2
Rg (real space) rg_real30.70
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real1.5290e+08
I(0) uncertainty (real space) i0_real_error2.3820e+06
Rg (reciprocal space) rg_reciprocal30.77
I(0) (reciprocal space) i0_reciprocal152900000.0000
Solution quality estimate total_estimate0.9129
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary40.6
Skewness Skewness skewness0.088
Kurtosis Kurtosis kurtosis-0.627
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha17950000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.967; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.963

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)