8x9s

Identification, structure and agonist design of an androgen membrane receptor.

Method: ELECTRON MICROSCOPY Dmax: 117.9 Å Quality: GOOD

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

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Rattus norvegicus

UniProt P54311

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 2–340 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Adhesion G-protein coupled receptor D1 × 1 (Q6QNK2) Gs protein alpha subunit × 1 DHT 5-ALPHA-DIHYDROTESTOSTERONE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

161 other PDB entries and 162 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 6–344; UniProt 2–340

Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2

Bos taurus

UniProt P63212

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain G; UniProt 1–71 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P54311) Adhesion G-protein coupled receptor D1 × 1 (Q6QNK2) Gs protein alpha subunit × 1 DHT 5-ALPHA-DIHYDROTESTOSTERONE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

215 other PDB entries and 216 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBG2_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–71; UniProt 1–71

Adhesion G-protein coupled receptor D1

Homo sapiens

UniProt Q6QNK2

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain R; UniProt 277–874 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P54311) Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Gs protein alpha subunit × 1 DHT 5-ALPHA-DIHYDROTESTOSTERONE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.49 Å

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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AGRD1_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain R; PDBConstruct 1–598; UniProt 277–874

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 8x9s

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8x9s
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8x9s
Deposition date deposition_date2023-12-01
Structure title titleIdentification, structure and agonist design of an androgen membrane receptor.
Keywords keywordsComplex, agonist, GPCR, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier34.21
Radius of gyration Rg (electron density) rg_electron34.15
Forward intensity I(0) i0142324000.00
Molecular weight molecular_weight96226.0 kDa
Excluded volume excluded_volume120810 ų
Envelope volume envelope_volume167710 ų
Hydration-shell volume shell_volume41912 ų
Envelope diameter envelope_diameter117.9
Shell Rg shell_rg39.47
Envelope Rg envelope_rg34.01
Shape Rg shape_rg34.13
Total Rg total_rg34.65
Total atoms total_atoms6774
Residues n_residues892
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 dmax117.9
Rg (real space) rg_real34.26
Rg uncertainty (real space) rg_real_error0.94
I(0) (real space) i0_real1.4230e+08
I(0) uncertainty (real space) i0_real_error2.1680e+06
Rg (reciprocal space) rg_reciprocal34.23
I(0) (reciprocal space) i0_reciprocal142300000.0000
Solution quality estimate total_estimate0.8738
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.9
Skewness Skewness skewness0.382
Kurtosis Kurtosis kurtosis-0.341
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha43020000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.829; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.975; Smooth: 0.894

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)