7fii

luteinizing hormone/choriogonadotropin receptor-chorionic gonadotropin-Gs complex

Method: ELECTRON MICROSCOPY Dmax: 170.5 Å Quality: REASONABLE

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 2–340 Not recorded Engineered Guanine nucleotide-binding protein G(s) subunit alpha × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2 × 1 (P63212) Lutropin-choriogonadotropic hormone receptor × 1 (P22888) Glycoprotein hormones alpha chain × 1 (P01215) Choriogonadotropin subunit beta 3 × 1 (P0DN86) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 2
Chains and sequence ranges Author chain B; PDBConstruct 12–350; 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain G; UniProt 1–71 Not recorded Engineered Guanine nucleotide-binding protein G(s) subunit alpha × 1 Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P54311) Lutropin-choriogonadotropic hormone receptor × 1 (P22888) Glycoprotein hormones alpha chain × 1 (P01215) Choriogonadotropin subunit beta 3 × 1 (P0DN86) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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 3
Chains and sequence ranges Author chain G; PDBConstruct 1–71; UniProt 1–71

Lutropin-choriogonadotropic hormone receptor

Homo sapiens

UniProt P22888

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain R; UniProt 28–699 Not recorded Engineered Guanine nucleotide-binding protein G(s) subunit alpha × 1 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) Glycoprotein hormones alpha chain × 1 (P01215) Choriogonadotropin subunit beta 3 × 1 (P0DN86) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LSHR_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain R; PDBConstruct 18–689; UniProt 28–699

Glycoprotein hormones alpha chain

Homo sapiens

UniProt P01215

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain X; UniProt 1–116 Not recorded Engineered Guanine nucleotide-binding protein G(s) subunit alpha × 1 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) Lutropin-choriogonadotropic hormone receptor × 1 (P22888) Choriogonadotropin subunit beta 3 × 1 (P0DN86) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

15 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GLHA_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain X; PDBConstruct 1–116; UniProt 1–116

Choriogonadotropin subunit beta 3

Homo sapiens

UniProt P0DN86

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain Y; UniProt 1–165 Not recorded Engineered Guanine nucleotide-binding protein G(s) subunit alpha × 1 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) Lutropin-choriogonadotropic hormone receptor × 1 (P22888) Glycoprotein hormones alpha chain × 1 (P01215) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.30 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CGB3_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain Y; PDBConstruct 1–165; UniProt 1–165

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 7fii

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7fii
Deposition date deposition_date2021-07-31
Structure title titleluteinizing hormone/choriogonadotropin receptor-chorionic gonadotropin-Gs complex
Keywords keywordsglycoprotein hormone receptor, chorionic gonadotropin, GPCR, Gs-protein, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.05
Radius of gyration Rg (electron density) rg_electron54.30
Forward intensity I(0) i0275288000.00
Molecular weight molecular_weight123530.0 kDa
Excluded volume excluded_volume148280 ų
Envelope volume envelope_volume288960 ų
Hydration-shell volume shell_volume48405 ų
Envelope diameter envelope_diameter177.3
Shell Rg shell_rg49.39
Envelope Rg envelope_rg54.28
Shape Rg shape_rg54.31
Total Rg total_rg54.08
Total atoms total_atoms8765
Residues n_residues1522
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 dmax170.5
Rg (real space) rg_real55.70
Rg uncertainty (real space) rg_real_error1.96
I(0) (real space) i0_real2.7530e+08
I(0) uncertainty (real space) i0_real_error6.2740e+06
Rg (reciprocal space) rg_reciprocal54.46
I(0) (reciprocal space) i0_reciprocal274800000.0000
Solution quality estimate total_estimate0.6987
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary35.3
Skewness Skewness skewness0.431
Kurtosis Kurtosis kurtosis-0.942
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15660000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.535; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.473; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)