3g8o

Progesterone Receptor with bound Pyrrolidine 1

Method: X-RAY DIFFRACTION Dmax: 87.0 Å Quality: EXCELLENT

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

Progesterone receptor

Homo sapiens

UniProt P06401

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 673–933 Chain B; UniProt 673–933 Fragment:ligand binding domain 30X N~2~-[4-cyano-3-(trifluoromethyl)phenyl]-N,N-dimethyl-N~2~-(2,2,2-trifluoroethyl)-L-alaninamide × 2 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:hanging drop;pH 7;298 K;0.1M Hepes, 0.2M Lithium Sulfate, 15% PEG3350, pH 7.0, hanging drop, temperature 298K Resolution 1.90 Å R-free 0.241

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.

18 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRGR_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–263; UniProt 673–933 Author chain B; PDBConstruct 3–263; UniProt 673–933

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 3g8o

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3g8o
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3g8o
Deposition date deposition_date2009-02-12
Structure title titleProgesterone Receptor with bound Pyrrolidine 1
Keywords keywords;Progesterone Receptor, Steroid Hormone Receptor, Nuclear Receptor, PR, progesterone, alpha helical sandwich, DNA-binding, Lipid-binding, Metal-binding, Nucleus, Phosphoprotein, Receptor, Steroid-binding, Transcription, Transcription regulation, Zinc-finger ;; TRANSCRIPTION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.38
Radius of gyration Rg (electron density) rg_electron26.43
Forward intensity I(0) i049354200.00
Molecular weight molecular_weight57401.0 kDa
Excluded volume excluded_volume73048 ų
Envelope volume envelope_volume87063 ų
Hydration-shell volume shell_volume27845 ų
Envelope diameter envelope_diameter94.4
Shell Rg shell_rg33.24
Envelope Rg envelope_rg26.41
Shape Rg shape_rg26.43
Total Rg total_rg27.19
Total atoms total_atoms4031
Residues n_residues500
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 dmax87.0
Rg (real space) rg_real27.39
Rg uncertainty (real space) rg_real_error0.48
I(0) (real space) i0_real4.9350e+07
I(0) uncertainty (real space) i0_real_error6.5040e+05
Rg (reciprocal space) rg_reciprocal27.39
I(0) (reciprocal space) i0_reciprocal49350000.0000
Solution quality estimate total_estimate0.9044
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.5
Skewness Skewness skewness0.293
Kurtosis Kurtosis kurtosis-0.602
Angular range angular_range— – 0.2900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha13560000.0000
Real-space data points n_real_points59
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.930; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3g8oa_
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_idd3g8ob_
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 (2 domains)

Domain ID domain_id3g8oA00
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology565 — Retinoid X Receptor
Homologous superfamily homologous superfamily10 — Retinoid X Receptor
Domain ID domain_id3g8oB00
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)